Enzyme Nomenclature

Continued from EC 1.3.1.51 to EC 1.3.1.111

EC 1.3.2 to EC 1.3.99

Sections

EC 1.3.2 With a cytochrome as acceptor
EC 1.3.3 With oxygen as acceptor
EC 1.3.4 With a disulfide as acceptor
EC 1.3.5 With a quinone or related compound as acceptor
EC 1.3.7 With an iron-sulfur protein as acceptor
EC 1.3.8 With flavin as acceptor
EC 1.3.98 With other, known, physiological acceptors
EC 1.3.99 With unknown physiological acceptors


EC 1.3.2 With a cytochrome as acceptor

Contents

EC 1.3.2.1 now EC 1.3.99.2
EC 1.3.2.2 now EC 1.3.99.3
EC 1.3.2.3 L-galactonolactone dehydrogenase


[EC 1.3.2.1 Transferred entry: now EC 1.3.99.2 butyryl-CoA dehydrogenase (EC 1.3.2.1 created 1961, deleted 1964)]

[EC 1.3.2.2 Transferred entry: now EC 1.3.99.3 acyl-CoA dehydrogenase (EC 1.3.2.2 created 1961, deleted 1964)]

EC 1.3.2.3

Accepted name: L-galactonolactone dehydrogenase

Reaction: L-galactono-1,4-lactone + 4 ferricytochrome c = L-dehydroascorbate + 4 ferrocytochrome c + 4 H+ (overall reaction)
(1a) L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c + 2 H+
(1b) L-ascorbate + 2 ferricytochrome c = L-dehydroascorbate + 2 ferrocytochrome c + 2 H+ (spontaneous)

Other name(s): galactonolactone dehydrogenase; L-galactono-γ-lactone dehydrogenase; L-galactono-γ-lactone:ferricytochrome-c oxidoreductase; GLDHase; GLDase

Systematic name: L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase

Comments: This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds [5]. The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-γ-lactone, D-gulono-γ-lactone, L-gulono-γ-lactone, D-erythronic-γ-lactone, D-xylonic-γ-lactone, L-mannono-γ-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates [5]. FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-02-1

References:

1. Mapson, L.W. and Breslow, E. Properties of partially purified L-galactono-γ-lactone dehydrogenase. Biochem. J. 65 (1957) 29 only.

2. Mapson, L.W., Isherwood, F.A. and Chen, Y.T. Biological synthesis of L-ascorbic acid: the conversion of L-galactono-γ-lactone into L-ascorbic acid by plant mitochondria. Biochem. J. 56 (1954) 21-28. [PMID: 13126087]

3. Isherwood, F.A., Chen, Y.T. and Mapson, L.W. Synthesis of L-ascorbic acid in plants and animals. Biochem. J. 56 (1954) 1-15. [PMID: 13126085]

4. Ôba, K., Ishikawa, S., Nishikawa, M., Mizuno, H. and Yamamoto, T. Purification and properties of L-galactono-γ-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots. J. Biochem. (Tokyo) 117 (1995) 120-124. [PMID: 7775377]

5. Østergaard, J., Persiau, G., Davey, M.W., Bauw, G. and Van Montagu, M. Isolation of a cDNA coding for L-galactono-γ-lactone dehydrogenase, an enzyme involved in the biosynthesis of ascorbic acid in plants. Purification, characterization, cDNA cloning, and expression in yeast. J. Biol. Chem. 272 (1997) 30009-30016. [PMID: 9374475]

[EC 1.3.2.3 created 1961, modified 2006]


EC 1.3.3 With oxygen as acceptor

Contents

EC 1.3.3.1 transferred now EC 1.3.98.1
EC 1.3.3.2 now EC 1.14.21.6
EC 1.3.3.3 coproporphyrinogen oxidase
EC 1.3.3.4 protoporphyrinogen oxidase
EC 1.3.3.5 bilirubin oxidase
EC 1.3.3.6 acyl-CoA oxidase
EC 1.3.3.7 dihydrouracil oxidase
EC 1.3.3.8 tetrahydroberberine oxidase
EC 1.3.3.9 secologanin synthase
EC 1.3.3.10 tryptophan α,β-oxidase
EC 1.3.3.11 pyrroloquinoline-quinone synthase
EC 1.3.3.12 L-galactonolactone oxidase
EC 1.3.3.13 albonoursin synthase
EC 1.3.3.14 aclacinomycin-A oxidase
EC 1.3.3.15 coproporphyrinogen III oxidase (coproporphyrin-forming)


[EC 1.3.3.1 Transferred entry: dihydroorotate oxidase. Now EC 1.3.98.1 dihydroorotate dehydrogenase (fumarate) (EC 1.3.3.1 created 1961, deleted 2011)]

[EC 1.3.3.2 Transferred entry: now EC 1.14.21.6, lathosterol oxidase. NAD(P)H had not been included previously, so enzyme had to be reclassified (EC 1.3.3.2 created 1972, deleted 2005)]

EC 1.3.3.3

Accepted name: coproporphyrinogen oxidase

Reaction: coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O

For diagram click here.

Other name(s): coproporphyrinogen III oxidase; coproporphyrinogenase

Systematic name: coproporphyrinogen:oxygen oxidoreductase (decarboxylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9076-84-0

References:

1. Battle, A.M., Benson, A. and Rimington, C. Purification and properties of coproporphyrinogenase. Biochem. J. 97 (1965) 731-740. [PMID: 5881662]

2. Medlock, A.E. and Dailey, H.A. Human coproporphyrinogen oxidase is not a metalloprotein. J. Biol. Chem. 271 (1996) 32507-32510. [PMID: 8955072]

3. Kohno, H., Furukawa, T., Yoshinaga, T., Tokunaga, R. and Taketani, S. Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. J. Biol. Chem. 268 (1993) 21359-21363. [PMID: 8407975]

[EC 1.3.3.3 created 1972, modified 2003]

EC 1.3.3.4

Accepted name: protoporphyrinogen oxidase

Reaction: protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2

For diagram click here.

Other name(s): protoporphyrinogen IX oxidase; protoporphyrinogenase; PPO; Protox; HemG; HemY

Systematic name: protoporphyrinogen-IX:oxygen oxidoreductase

Comments: This is the last common enzyme in the biosynthesis of chlorophylls and heme [8]. Two isoenzymes exist in plants: one in plastids and the other in mitochondria. This is the target enzyme of phthalimide-type and diphenylether-type herbicides [8]. The enzyme from oxygen-dependent species contains FAD [9]. Also slowly oxidizes mesoporphyrinogen IX.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 53986-32-6

References:

1. Poulson, R. The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX in mammalian mitochondria. J. Biol. Chem. 251 (1976) 3730-3733. [PMID: 6461]

2. Poulson, R. and Polglase, W.J. The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae. J. Biol. Chem. 250 (1975) 1269-1274. [PMID: 234450]

3. Dailey, H.A. and Dailey, T.A. Protoporphyrinogen oxidase of Myxococcus xanthus. Expression, purification, and characterization of the cloned enzyme. J. Biol. Chem. 271 (1996) 8714-8718. [PMID: 8621504]

4. Wang, K.F., Dailey, T.A. and Dailey, H.A. Expression and characterization of the terminal heme synthetic enzymes from the hyperthermophile Aquifex aeolicus. FEMS Microbiol. Lett. 202 (2001) 115-119. [PMID: 11506917]

5. Corrigall, A.V., Siziba, K.B., Maneli, M.H., Shephard, E.G., Ziman, M., Dailey, T.A., Dailey, H.A., Kirsch. R.E. and Meissner, P.N. Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis. Arch. Biochem. Biophys. 358 (1998) 251-256. [PMID: 9784236]

6. Ferreira, G.C. and Dailey, H.A. Mouse protoporphyrinogen oxidase. Kinetic parameters and demonstration of inhibition by bilirubin. Biochem. J. 250 (1988) 597–603. [PMID: 2451512]

7. Dailey, T.A. and Dailey, H.A. Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme. Protein Sci. 5 (1996) 98–105. [PMID: 8771201]

8. Che, F.S., Watanabe, N., Iwano, M., Inokuchi, H., Takayama, S., Yoshida, S. and Isogai, A. Molecular characterization and subcellular localization of protoporphyrinogen oxidase in spinach chloroplasts. Plant Physiol. 124 (2000) 59–70. [PMID: 10982422]

9. Dailey, T.A. and Dailey, H.A. Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus. J. Biol. Chem. 273 (1998) 13658–13662. [PMID: 9593705]

[EC 1.3.3.4 created 1978, modified 2003]

EC 1.3.3.5

Accepted name: bilirubin oxidase

Reaction: 2 bilirubin + O2 = 2 biliverdin + 2 H2O

For diagram click here.

Other name(s): bilirubin oxidase M-1

Systematic name: bilirubin:oxygen oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 80619-01-8

References:

1. Murao, S. and Tanaka, N. A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agric. Biol. Chem. 45 (1981) 2383-2384.

2. Tanaka, N. and Murao, S. Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agr. Biol. Chem. 49 (1985) 843-844.

[EC 1.3.3.5 created 1984]

EC 1.3.3.6

Accepted name: acyl-CoA oxidase

Reaction: acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2

Other name(s): fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase

Systematic name: acyl-CoA:oxygen 2-oxidoreductase

Comments: A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 61116-22-1

References:

1. Kawaguchi, A., Tsubotani, S., Seyama, Y., Yamakawa, T., Osumi, T., Hashimoto, T., Kikuchi, T., Ando, M. and Okuda, S. Stereochemistry of dehydrogenation catalyzed by acyl-CoA oxidase. J. Biochem. (Tokyo) 88 (1980) 1481-1486. [PMID: 7462191]

2. Osumi, T., Hashimoto, T. and Ui, N. Purification and properties of acyl-CoA oxidase from rat liver. J. Biochem. (Tokyo) 87 (1980) 1735-1746. [PMID: 7400120]

[EC 1.3.3.6 created 1986]

EC 1.3.3.7

Accepted name: dihydrouracil oxidase

Reaction: 5,6-dihydrouracil + O2 = uracil + H2O2

Systematic name: 5,6-dihydrouracil:oxygen oxidoreductase

Comments: Also oxidizes dihydrothymine to thymine. A flavoprotein (FMN).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104327-11-9

References:

1. Owaki, J., Uzura, K., Minami, Z. and Kusai, K. Partial-purification and characterization of dihydrouracil oxidase, a flavoprotein from Rhodotorula glutinis. J. Ferment. Technol. 64 (1986) 205-210.

[EC 1.3.3.7 created 1989]

EC 1.3.3.8

Accepted name: tetrahydroberberine oxidase

Reaction: (S)-tetrahydroberberine + 2 O2 = berberine + 2 H2O2

For diagram click here or here.

Other name(s): (S)-THB oxidase

Systematic name: (S)-tetrahydroberberine:oxygen oxidoreductase

Comments: The enzyme from Berberis sp. (previously listed as EC 1.5.3.8) is a flavoprotein; that from Coptis japonica is not. (R)-Tetrahydroberberines are not oxidized.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114705-00-9

References:

1. Amann, M., Nagakura, N. and Zenk, M.H. (S)-Tetrahydroprotoberberine oxidase the final enzyme in protoberberine biosynthesis. Tetrahedron Lett. 25 (1984) 953-954.

2. Okada, N., Shinmyo, A., Okada, H. and Yamada, Y. Purification and characterization of (S)-tetrahydroberberine oxidase from cultured Coptis japonica cells. Phytochemistry 27 (1988) 979-982.

[EC 1.3.3.8 created 1990 (EC 1.5.3.8 created 1989, incorporated 1992)]

EC 1.3.3.9

Accepted name: secologanin synthase

Reaction: loganin + NADPH + H+ + O2 = secologanin + NADP+ + 2 H2O

For diagram click here.

Systematic name: loganin:oxygen oxidoreductase (ring-cleaving)

Comments: A heme-thiolate protein (P-450). Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 258339-71-8

References:

1. Yamamoto, H., Katano, N., Ooi, A. and Inoue, K. Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P-450. Phytochemistry 53 (2000) 7-12. [PMID: 10656401]

2. Irmler, S., Schroder, G., St-Pierre, B., Crouch, N.P., Hotze, M., Schmidt, J., Strack, D., Matern, U. and Schroder, J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P-450 CYP72A1 as secologanin synthase. Plant J. 24 (2000) 797-804. [PMID: 11135113]

3. Yamamoto, H., Katano, N., Ooi, Y. and Inoue, K. Transformation of loganin and 7-deoxyloganin into secologanin by Lonicera japonica cell suspension cultures Phytochemistry 50 (1999) 417-422.

[EC 1.3.3.9 created 2002]

EC 1.3.3.10

Accepted name: tryptophan α,β-oxidase

Reaction: L-tryptophan + O2 = α,β-didehydrotryptophan + H2O2

Other name(s): L-tryptophan 2',3'-oxidase; L-tryptophan α,β-dehydrogenase

Systematic name: L-tryptophan:oxygen α,β-oxidoreductase

Comments: Requires heme. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Also catalyses the α,β dehydrogenation of L-tryptophan side chains in peptides. The product of the reaction can hydrolyse spontaneously to form indolepyruvate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 156859-19-7

References:

1. Genet, R., Denoyelle, C. and Menez, A. Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. J. Biol. Chem. 269 (1994) 18177-18184. [PMID: 8027079]

2. Genet, R., Benetti, P.H., Hammadi, A. and Menez, A. L-Tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem. 270 (1995) 23540-23545. [PMID: 7559518]

[EC 1.3.3.10 created 2000 as EC 1.4.3.17, transferred 2003 to EC 1.3.3.10]

EC 1.3.3.11

Accepted name: pyrroloquinoline-quinone synthase

Reaction: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O

For diagram click here.

Other name(s): PqqC

Systematic name: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-octahydroquinoline-2,4-dicarboxylate:oxygen oxidoreductase (cyclizing)

Comments: So far only a single turnover of the enzyme has been observed, and the pyrroloquinoline quinone remains bound to it. It is not yet known what releases the product in the bacterium.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 353484-42-1

References:

1. Magnusson, O.T., Toyama, H., Saeki, M., Schwarzenbacher, R. and Klinman, J.P. The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis. J. Am. Chem. Soc. 126 (2004) 5342-5343. [PMID: 15113189]

2. Magnusson, O.T., Toyama, H., Saeki, M., Rojas, A., Reed, J.C., Liddington, R.C., Klinman, J.P. and Schwarzenbacher, R. Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone. Proc. Natl. Acad. Sci. USA 101 (2004) 7913-7918. [PMID: 15148379]

3. Toyama, H., Chistoserdova, L. and Lidstrom, M.E. Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate. Microbiology 143 (1997) 595-602. [PMID: 9043136]

4. Toyama, H., Fukumoto, H., Saeki, M., Matsushita, K., Adachi, O. and Lidstrom, M.E. PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone. Biochem. Biophys. Res. Commun. 299 (2002) 268-272. [PMID: 1243798]

5. Schwarzenbacher, R., Stenner-Liewen, F., Liewen, H., Reed, J.C. and Liddington, R.C. Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 Å resolution. Protein 56 (2004) 401-403. [PMID: 15211525]

[EC 1.3.3.11 created 2005]

EC 1.3.3.12

Accepted name: L-galactonolactone oxidase

Reaction: L-galactono-1,4-lactone + O2 = L-ascorbate + H2O2

Other name(s): L-galactono-1,4-lactone oxidase

Systematic name: L-galactono-1,4-lactone:oxygen 3-oxidoreductase

Comments: A flavoprotein. Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, D-arabinic and D-threonic acids; not identical with EC 1.1.3.8 L-gulonolactone oxidase. (cf. EC 1.3.2.3 galactonolactone dehydrogenase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bleeg, H.S. and Christensen, F. Biosynthesis of ascorbate in yeast. Purification of L-galactono-1,4-lactone oxidase with properties different from mammalian L-gulonolactone oxidase. Eur. J. Biochem. 127 (1982) 391-396. [PMID: 6754380]

[EC 1.3.3.12 created 1984 as EC 1.1.3.24, transferred 2006 to EC 1.3.3.12]

EC 1.3.3.13

Accepted name: albonoursin synthase

Reaction: cyclo(L-leucyl-L-phenylalanyl) + 2 O2 = albonoursin + 2 H2O2 (overall reaction)
(1a) cyclo(L-leucyl-L-phenylalanyl) + O2 = cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] + H2O2
(1b) cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] + O2 = albonoursin + H2O2

For diagram of reaction click here.

Glossary: cyclo(L-leucyl-L-phenylalanyl) = (3S,6S)-3-benzyl-6-(2-methylpropyl)piperazine-2,5-dione
cyclo[(Z)-α,β-didehydrophenylalanyl-L-leucyl] = (3Z,6S)-3-benzylidene-6-(2-methylpropyl)piperazine-2,5-dione
albonoursin = (3Z,6Z)-3-benzylidene-6-(2-methylpropylidene)piperazine-2,5-dione

Other name(s): cyclo(dipeptide):oxygen oxidoreductase; cyclic dipeptide oxidase; AlbA

Systematic name: cyclo(L-leucyl-L-phenylalanyl):oxygen oxidoreductase

Comments: A flavoprotein from the bacterium Streptomyces noursei. The enzyme can also oxidize several other cyclo dipeptides, the best being cyclo(L-tryptophyl-L-tryptophyl) and cyclo(L-phenylalanyl-L-phenylalanyl) [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Gondry, M., Lautru, S., Fusai, G., Meunier, G., Menez, A. and Genet, R. Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl α,β-dehydrogenase. Eur. J. Biochem. 268 (2001) 1712-1721. [PMID: 11248691]

2. Lautru, S., Gondry, M., Genet, R. and Pernodet, J.L. The albonoursin gene cluster of S. noursei. Biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases. Chem. Biol. 9 (2002) 1355-1364. [PMID: 12498889]

[EC 1.3.3.13 created 2013]

EC 1.3.3.14

Accepted name: aclacinomycin-A oxidase

Reaction: aclacinomycin A + O2 = aclacinomycin Y + H2O2

For diagram of reaction click here.

Glossary: aclacinomycin A = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-tetrahydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester
aclacinomycin Y = 2-ethyl-1,2,3,4,6,11-hexahydro-2,5,7-trihydroxy-6,11-dioxo-4-[[2,3,6-trideoxy-4-O-[2,6-dideoxy-4-O-[(2R,6S)-5,6-dihydro-6-methyl-5-oxo-2H-pyran-2-yl]-α-L-lyxo-hexopyranosyl]-3-(dimethylamino)-α-L-lyxo-hexopyranosyl]oxy]naphthacene-1-carboxylic acid methyl ester

Other name(s): AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous)

Systematic name: aclacinomycin-A:oxygen oxidoreductase

Comments: A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Yoshimoto, A., Ogasawara, T., Kitamura, I., Oki, T., Inui, T., Takeuchi, T. and Umezawa, H. Enzymatic conversion of aclacinomycin A to Y by a specific oxidoreductase in Streptomyces. J. Antibiot. (Tokyo) 32 (1979) 472-481. [PMID: 528393]

2. Alexeev, I., Sultana, A., Mantsala, P., Niemi, J. and Schneider, G. Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual flavoenzyme with a dual active site. Proc. Natl. Acad. Sci. USA 104 (2007) 6170-6175. [PMID: 17395717]

3. Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J. and Schneider, G. Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 149-159. [PMID: 17242508]

[EC 1.3.3.14 created 2013]

EC 1.3.3.15

Accepted name: coproporphyrinogen III oxidase (coproporphyrin-forming)

Reaction: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2

Other name(s): hemY (gene name)

Systematic name: coproporphyrinogen-III:oxygen oxidoreductase (coproporphyrin-forming)

Comments: Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Hansson, M. and Hederstedt, L. Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX. J. Bacteriol. 176 (1994) 5962-5970. [PMID: 7928957]

2. Corrigall, A.V., Siziba, K.B., Maneli, M.H., Shephard, E.G., Ziman, M., Dailey, T.A., Dailey, H.A., Kirsch, R.E. and Meissner, P.N. Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis. Arch. Biochem. Biophys. 358 (1998) 251-256. [PMID: 9784236]

3. Qin, X., Sun, L., Wen, X., Yang, X., Tan, Y., Jin, H., Cao, Q., Zhou, W., Xi, Z. and Shen, Y. Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis. J. Struct. Biol. 170 (2010) 76-82. [PMID: 19944166]

4. Dailey, H.A., Gerdes, S., Dailey, T.A., Burch, J.S. and Phillips, J.D. Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin. Proc. Natl. Acad. Sci. USA 112 (2015) 2210-2215. [PMID: 25646457]

[EC 1.3.3.15 created 2016]


EC 1.3.4 With a disulfide as acceptor

EC 1.3.4.1

Accepted name: fumarate reductase (CoM/CoB)

Reaction: fumarate + CoM + CoB = succinate + CoM-S-S-CoB

Glossary: CoB = coenzyme B = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate = N-(7-thioheptanoyl)-3-O-phosphothreonine
CoM = coenzyme M = 2-mercaptoethanesulfonate

Other name(s): thiol:fumarate reductase; Tfr

Systematic name: fumarate CoM:CoB oxidoreductase (succinate-forming)

Comments: The enzyme, isolated from the archaeon Methanobacterium thermoautotrophicum, is very oxygen sensitive. It cannot use reduced flavins, reduced coenzyme F420, or NAD(P)H as an electron donor. Distinct from EC 1.3.1.6 [fumarate reductase (NADH)], EC 1.3.5.1 [succinate dehydrogenase (ubiquinone)], and EC 1.3.5.4 [fumarate reductase (quinol)].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Khandekar, S.S. and Eirich, L.D. Purification and characterization of an anabolic fumarate reductase from Methanobacterium thermoautotrophicum. Appl. Environ. Microbiol. 55 (1989) 856-861. [PMID: 2499256]

2. Heim, S., Kunkel, A., Thauer, R.K. and Hedderich, R. Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum. Identification of the catalytic sites for fumarate reduction and thiol oxidation. Eur. J. Biochem. 253 (1998) 292-299. [PMID: 9578488]

[EC 1.3.4.1 created 2014 as EC 1.3.98.2, transferred 2014 to EC 1.3.4.1]


EC 1.3.5 With a quinone or related compound as acceptor

EC 1.3.5.1 succinate dehydrogenase (quinone)
EC 1.3.5.2 dihydroorotate dehydrogenase (quinone)
EC 1.3.5.3 protoporphyrinogen IX dehydrogenase (menaquinone)
EC 1.3.5.4 fumarate reductase (quinol)
EC 1.3.5.5 15-cis-phytoene desaturase
EC 1.3.5.6 9,9'-dicis-ζ-carotene desaturase

EC 1.3.5.1

Accepted name: succinate dehydrogenase (quinone)

Reaction: succinate + a quinone = fumarate + a quinol

For diagram of reaction click here.

Other name(s): succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase

Systematic name: succinate:quinone oxidoreductase

Comments: A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone cf. EC 1.3.5.4, fumarate reductase (quinone).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-11-9

References:

1. Kita, K., Vibat, C.R., Meinhardt, S., Guest, J.R. and Gennis, R.B. One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556. J. Biol. Chem. 264 (1989) 2672-2677. [PMID: 2644269]

2. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1-70.

3. Moll, R. and Schafer, G. Purification and characterisation of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius. Eur. J. Biochem. 201 (1991) 593–600. [PMID: 1935955]

4. Figueroa, P., Leon, G., Elorza, A., Holuigue, L., Araya, A. and Jordana, X. The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana. Plant Mol. Biol. 50 (2002) 725-734. [PMID: 12374303]

5. Cecchini, G. Function and structure of complex II of the respiratory chain. Annu. Rev. Biochem. 72 (2003) 77-109. [PMID: 14527321]

6. Oyedotun, K.S. and Lemire, B.D. The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies. J. Biol. Chem. 279 (2004) 9424-9431. [PMID: 14672929]

7. Kurokawa, T. and Sakamoto, J. Purification and characterization of succinate:menaquinone oxidoreductase from Corynebacterium glutamicum. Arch. Microbiol. 183 (2005) 317-324. [PMID: 15883782]

[EC 1.3.5.1 created 1983, modified 2014]

EC 1.3.5.2

Accepted name: dihydroorotate dehydrogenase (quinone)

Reaction: (S)-dihydroorotate + a quinone = orotate + a quinol

Other name(s): dihydroorotate:ubiquinone oxidoreductase; (S)-dihydroorotate:(acceptor) oxidoreductase; (S)-dihydroorotate:acceptor oxidoreductase; DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); DHODH

Systematic name: (S)-dihydroorotate:quinone oxidoreductase

Comments: This Class 2 dihydroorotate dehydrogenase enzyme contains FMN [4]. The enzyme is found in eukaryotes in the mitochondrial membrane, and in some Gram negative bacteria associated with the cytoplasmic membrane [2,5]. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides [2,4]. The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates [2]. Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but 1- and 3-methyl and 1,3-dimethyl methyl-(S)-dihydroorotates are not [2]. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 59088-23-2

References:

1. Forman, H.J. and Kennedy, J. Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme. Arch. Biochem. Biophys. 191 (1978) 23-31. [PMID: 216313]

2. Hines, V., Keys, L.D., III and Johnston, M. Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase. J. Biol. Chem. 261 (1986) 11386-11392. [PMID: 3733756]

3. Bader, B., Knecht, W., Fries, M. and Löffler, M. Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase. Protein Expr. Purif. 13 (1998) 414-422. [PMID: 9693067]

4. Fagan, R.L., Nelson, M.N., Pagano, P.M. and Palfey, B.A. Mechanism of flavin reduction in Class 2 dihydroorotate dehydrogenases. Biochemistry 45 (2006) 14926-14932. [PMID: 17154530]

5. Björnberg, O., Grüner, A.C., Roepstorff, P. and Jensen, K.F. The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry 38 (1999) 2899-2908. [PMID: 10074342]

[EC 1.3.5.2 created 1983 as EC 1.3.99.11, transferred 2009 to EC 1.3.5.2, modified 2011]

EC 1.3.5.3

Accepted name: protoporphyrinogen IX dehydrogenase (menaquinone)

Reaction: protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

Other name(s): HemG

Systematic name: protoporphyrinogen IX:menaquinone oxidoreductase

Comments: This enzyme enables Escherichia coli to synthesize heme in both aerobic and anaerobic environments.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Boynton, T.O., Daugherty, L.E., Dailey, T.A. and Dailey, H.A. Identification of Escherichia coli HemG as a novel, menadione-dependent flavodoxin with protoporphyrinogen oxidase activity. Biochemistry 48 (2009) 6705-6711. [PMID: 19583219]

[EC 1.3.5.3 created 2010]

EC 1.3.5.4

Accepted name: fumarate reductase (quinol)

Reaction: succinate + a quinone = fumarate + a quinol

Other name(s): FRD; menaquinol-fumarate oxidoreductase; succinate dehydrogenase (menaquinone); succinate:menaquinone oxidoreductase; fumarate reductase (menaquinone); complex II (ambiguous)

Systematic name: succinate:quinone oxidoreductase

Comments: The reaction is catalysed in the opposite direction. The enzyme, which is found in anaerobic and facultative organisms such as bacteria, parasitic helminthes, and lower marine organisms, utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain. The enzyme is known as complex II of the electron transfer chain, similarly to EC 1.3.5.1, succinate dehydrogenase (quinone), to which it is closely related.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Van Hellemond, J.J. and Tielens, A.G. Expression and functional properties of fumarate reductase. Biochem. J. 304 (1994) 321-331. [PMID: 7998964]

2. Iverson, T.M., Luna-Chavez, C., Cecchini, G. and Rees, D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284 (1999) 1961-1966. [PMID: 10373108]

3. Cecchini, G., Schroder, I., Gunsalus, R.P. and Maklashina, E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim. Biophys. Acta 1553 (2002) 140-157. [PMID: 11803023]

4. Iverson, T.M., Luna-Chavez, C., Croal, L.R., Cecchini, G. and Rees, D.C. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J. Biol. Chem. 277 (2002) 16124-16130. [PMID: 11850430]

5. van Hellemond, J.J., van der Klei, A., van Weelden, S.W. and Tielens, A.G. Biochemical and evolutionary aspects of anaerobically functioning mitochondria. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358 (2003) 205. [PMID: 12594928]

[EC 1.3.5.4 created 2010, modified 2013]

EC 1.3.5.5

Accepted name: 15-cis-phytoene desaturase

Reaction: 15-cis-phytoene + 2 plastoquinone = 9,15,9'-tricis-ζ-carotene + 2 plastoquinol (overall reaction)
(1a) 15-cis-phytoene + plastoquinone = 15,9'-dicis-phytofluene + plastoquinol
(1b) 15,9'-dicis-phytofluene + plastoquinone = 9,15,9'-tricis-ζ-carotene + plastoquinol

For diagram of reaction click here.

Other name(s): phytoene desaturase (ambiguous); PDS; plant-type phytoene desaturase

Systematic name: 15-cis-phytoene:plastoquinone oxidoreductase

Comments: This enzyme is involved in carotenoid biosynthesis in plants and cyanobacteria. The enzyme from Synechococcus can also use NAD+ and NADP+ as electron acceptor under anaerobic conditions. The enzyme from Gentiana lutea shows no activity with NAD+ or NADP+ [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Breitenbach, J., Zhu, C. and Sandmann, G. Bleaching herbicide norflurazon inhibits phytoene desaturase by competition with the cofactors. J. Agric. Food Chem. 49 (2001) 5270-5272. [PMID: 11714315]

2. Schneider, C., Boger, P. and Sandmann, G. Phytoene desaturase: heterologous expression in an active state, purification, and biochemical properties. Protein Expr. Purif. 10 (1997) 175-179. [PMID: 9226712]

3. Fraser, P.D., Linden, H. and Sandmann, G. Purification and reactivation of recombinant Synechococcus phytoene desaturase from an overexpressing strain of Escherichia coli. Biochem. J. 291 (1993) 687-692. [PMID: 8489496]

4. Breitenbach, J. and Sandmann, G. ζ-Carotene cis isomers as products and substrates in the plant poly-cis carotenoid biosynthetic pathway to lycopene. Planta 220 (2005) 785-793. [PMID: 15503129]

[EC 1.3.5.5 created 2011]

EC 1.3.5.6

Accepted name: 9,9'-dicis-ζ-carotene desaturase

Reaction: 9,9'-dicis-ζ-carotene + 2 quinone = 7,9,7',9'-tetracis-lycopene + 2 quinol (overall reaction)
(1a) 9,9'-dicis-ζ-carotene + a quinone = 7,9,9'-tricis-neurosporene + a quinol
(1b) 7,9,9'-tricis-neurosporene + a quinone = 7,9,7',9'-tetracis-lycopene + a quinol

For diagram of reaction click here.

Glossary: 7,9,7',9'-tetracis-lycopene = prolycopene

Other name(s): ζ-carotene desaturase; ZDS

Systematic name: 9,9'-dicis-ζ-corotene:quinone oxidoreductase

Comments: This enzyme is involved in carotenoid biosynthesis in plants and cyanobacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Albrecht, M., Linden, H. and Sandmann, G. Biochemical characterization of purified ζ-carotene desaturase from Anabaena PCC 7120 after expression in E. coli. Eur. J. Biochem. 236 (1996) 115-120. [PMID: 8617254]

2. Josse, E.M., Simkin, A.J., Gaffe, J., Laboure, A.M., Kuntz, M. and Carol, P. A plastid terminal oxidase associated with carotenoid desaturation during chromoplast differentiation. Plant Physiol. 123 (2000) 1427-1436. [PMID: 10938359]

3. Breitenbach, J., Kuntz, M., Takaichi, S. and Sandmann, G. Catalytic properties of an expressed and purified higher plant type ζ-carotene desaturase from Capsicum annuum. Eur. J. Biochem. 265 (1999) 376-383. [PMID: 10491195]

4. Breitenbach, J. and Sandmann, G. ζ-Carotene cis isomers as products and substrates in the plant poly-cis carotenoid biosynthetic pathway to lycopene. Planta 220 (2005) 785-793. [PMID: 15503129]

[EC 1.3.5.6 created 1999 as EC 1.14.99.30, transferred 2011 to EC 1.3.5.6]


EC 1.3.7 With an iron-sulfur protein as acceptor

Contents

EC 1.3.7.1 6-hydroxynicotinate reductase
EC 1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
EC 1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductase
EC 1.3.7.4 phytochromobilin:ferredoxin oxidoreductase
EC 1.3.7.5 phycocyanobilin:ferredoxin oxidoreductase EC 1.3.7.6 phycoerythrobilin synthase
EC 1.3.7.7 ferredoxin:protochlorophyllide reductase (ATP-dependent)
EC 1.3.7.8 benzoyl-CoA reductase
EC 1.3.7.9 4-hydroxybenzoyl-CoA reductase
EC 1.3.7.10 transferred now EC 1.14.19.8
EC 1.3.7.11 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
EC 1.3.7.12 red chlorophyll catabolite reductase
EC 1.3.7.13 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin)
EC 1.3.7.14 3,8-divinyl chlorophyllide a reductase
EC 1.3.7.15 chlorophyllide a reductase

EC 1.3.7.1

Accepted name: 6-hydroxynicotinate reductase

Reaction: 6-oxo-1,4,5,6-tetrahydronicotinate + oxidized ferredoxin = 6-hydroxynicotinate + reduced ferredoxin

For diagram click here.

Other name(s): 6-oxotetrahydronicotinate dehydrogenase; 6-hydroxynicotinic reductase; HNA reductase

Systematic name: 6-oxo-1,4,5,6-tetrahydronicotinate:ferredoxin oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9030-84-6

References:

1. Holcenberg, J.S. and Tsai, L. Nicotinic acid metabolism. IV. Ferredoxin-dependent reduction of 6-hydroxynicotinic acid to 6-oxo-1,4,5,6-tetrahydronicotinic acid. J. Biol. Chem. 244 (1969) 1204-1211. [PMID: 5767303]

[EC 1.3.7.1 created 1972]

EC 1.3.7.2

Accepted name: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

Reaction: 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXα + reduced ferredoxin

For diagram click here.

Other name(s): PebA

Systematic name: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

Comments: Catalyses the two-electron reduction of biliverdin IXα at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα into phycoerythrobilin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 347401-20-1

References:

1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]

[EC 1.3.7.2 created 2002]

EC 1.3.7.3

Accepted name: phycoerythrobilin:ferredoxin oxidoreductase

Reaction: (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin

For diagram click here.

Other name(s): PebB

Systematic name: (3Z)-phycoerythrobilin:ferredoxin oxidoreductase

Comments: Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα to phycoerythrobilin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 347401-21-2

References:

1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]

[EC 1.3.7.3 created 2002]

EC 1.3.7.4

Accepted name: phytochromobilin:ferredoxin oxidoreductase

Reaction: (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXα + reduced ferredoxin

For diagram click here.

Other name(s): HY2; PΦB synthase; phytochromobilin synthase

Systematic name: (3Z)-phytochromobilin:ferredoxin oxidoreductase

Comments: Catalyses the two-electron reduction of biliverdin IXα. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 138263-99-7

References:

1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]

2. McDowell, M.T. and Lagarias, J.C. Purification and biochemical properties of phytochromobilin synthase from etiolated oat seedlings. Plant Physiol. 126 (2001) 1546-1554. [PMID: 11500553]

3. Terry, M.J., Wahleithner, J.A. and Lagarias, J.C. Biosynthesis of the plant photoreceptor phytochrome. Arch. Biochem. Biophys. 306 (1993) 1-15. [PMID: 8215388]

[EC 1.3.7.4 created 2002]

EC 1.3.7.5

Accepted name: phycocyanobilin:ferredoxin oxidoreductase

Reaction: (3Z)-phycocyanobilin + 4 oxidized ferredoxin = biliverdin IXα + 4 reduced ferredoxin

For diagram of reaction click here.

Systematic name: (3Z)-phycocyanobilin:ferredoxin oxidoreductase

Comments: Catalyses the four-electron reduction of biliverdin IXα (2-electron reduction at both the A and D rings). Reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. Flavodoxins can be used instead of ferredoxin. The direct conversion of biliverdin IXα (BV) to (3Z)-phycocyanolbilin (PCB) in the cyanobacteria Synechocystis sp. PCC 6803, Anabaena sp. PCC7120 and Nostoc punctiforme is in contrast to the proposed pathways of PCB biosynthesis in the red alga Cyanidium caldarium, which involves (3Z)-phycoerythrobilin (PEB) as an intermediate [2] and in the green alga Mesotaenium caldariorum, in which PCB is an isolable intermediate.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 347401-12-1

References:

1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]

2. Beale, S.I. Biosynthesis of phycobilins. Chem. Rev. 93 (1993) 785-802.

3. Wu, S.-H., McDowell, M.T. and Lagarias, J.C. Phycocyanobilin is the natural chromophore precursor of phytochrome from the green alga Mesotaenium caldariorum. J. Biol. Chem. 272 (1997) 25700-25705. [PMID: 9325294]

[EC 1.3.7.5 created 2002, modified 2014]

EC 1.3.7.6

Accepted name: phycoerythrobilin synthase

Reaction: (3Z)-phycoerythrobilin + 2 oxidized ferredoxin = biliverdin IXα + 2 reduced ferredoxin

Other name(s): PebS

Systematic name: (3Z)-phycoerythrobilin:ferredoxin oxidoreductase (from biliverdin IXα)

Comments: This enzyme, from a cyanophage infecting oceanic cyanobacteria of the Prochlorococcus genus, uses a four-electron reduction to carry out the reactions catalysed by EC 1.3.7.2 (15,16-dihydrobiliverdin:ferredoxin oxidoreductase) and EC 1.3.7.3 (phycoerythrobilin:ferredoxin oxidoreductase). 15,16-Dihydrobiliverdin is formed as a bound intermediate. Free 15,16-dihydrobiliverdin can also act as a substrate to form phycoerythrobilin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Dammeyer, T., Bagby, S.C., Sullivan, M.B., Chisholm, S.W. and Frankenberg-Dinkel, N. Efficient phage-mediated pigment biosynthesis in oceanic cyanobacteria. Curr. Biol. 18 (2008) 442-448. [PMID: 18356052]

[EC 1.3.7.6 created 2008]

EC 1.3.7.7

Accepted name: ferredoxin:protochlorophyllide reductase (ATP-dependent)

Reaction: chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O

For diagram of reaction click here.

Other name(s): light-independent protochlorophyllide reductase

Systematic name: ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase

Comments: Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Fujita, Y., Matsumoto, H., Takahashi, Y. and Matsubara, H. Identification of a nifDK-like gene (ORF467) involved in the biosynthesis of chlorophyll in the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 34 (1993) 305-314. [PMID: 8199775]

2. Nomata, J., Ogawa, T., Kitashima, M., Inoue, K. and Fujita, Y. NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters. FEBS Lett. 582 (2008) 1346-1350. [PMID: 18358835]

3. Muraki, N., Nomata, J., Ebata, K., Mizoguchi, T., Shiba, T., Tamiaki, H., Kurisu, G. and Fujita, Y. X-ray crystal structure of the light-independent protochlorophyllide reductase. Nature 465 (2010) 110-114. [PMID: 20400946]

[EC 1.3.7.7 created 2011, modified 2013]

EC 1.3.7.8

Accepted name: benzoyl-CoA reductase

Reaction: cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O

For diagram of reaction click here.

Other name(s): benzoyl-CoA reductase (dearomatizing)

Systematic name: cyclohexa-1,5-diene-1-carbonyl-CoA:ferredoxin oxidoreductase (aromatizing, ATP-forming)

Comments: An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 176591-18-7

References:

1. Boll, M. and Fuchs, G. Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172. Eur. J. Biochem. 234 (1995) 921-933. [PMID: 8575453]

2. Kung, J.W., Baumann, S., von Bergen, M., Muller, M., Hagedoorn, P.L., Hagen, W.R. and Boll, M. Reversible biological Birch reduction at an extremely low redox potential. J. Am. Chem. Soc. 132 (2010) 9850-9856. [PMID: 20578740]

[EC 1.3.7.8 created 1999 as EC 1.3.99.15, transferred 2011 to EC 1.3.7.8, modified 2011]

EC 1.3.7.9

Accepted name: 4-hydroxybenzoyl-CoA reductase

Reaction: benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin

Other name(s): 4-hydroxybenzoyl-CoA reductase (dehydroxylating); 4-hydroxybenzoyl-CoA:(acceptor) oxidoreductase

Systematic name: benzoyl-CoA:acceptor oxidoreductase

Comments: A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria. A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 133758-58-4

References:

1. Glockler, R., Tschech, A. and Fuchs, G. Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species. FEBS Lett. 251 (1989) 237-240. [PMID: 2753161]

2. Heider, J., Boll, M., Breese, K., Breinig, S., Ebenau-Jehle, C., Feil, U., Gad'on, N., Laempe, D., Leuthner, B., Mohamed, M.E.S., Schneider, S., Burchhardt, G. and Fuchs, G. Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica. Arch. Microbiol. 170 (1998) 120-131. [PMID: 9683649]

3. Breese, K. and Fuchs, G. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins. Eur. J. Biochem. 251 (1998) 916-923. [PMID: 9490068]

4. Brackmann, R. and Fuchs, G. Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species. Eur. J. Biochem. 213 (1993) 563-571. [PMID: 8477729]

5. Heider, J. and Fuchs, G. Anaerobic metabolism of aromatic compounds. Eur. J. Biochem. 243 (1997) 577-596. [PMID: 9057820]

[EC 1.3.7.9 created 2000 as EC 1.3.99.20, transferred 2011 to EC 1.3.7.9]

[EC 1.3.7.10 Transferred entry: pentalenolactone synthase. Now classified as EC 1.14.19.8, pentalenolactone synthase (EC 1.3.7.10 created 2012, deleted 2013)]

EC 1.3.7.11

Accepted name: 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase

Reaction: a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized ferredoxin [iron-sulfur] cluster = a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+

For diagram of reaction click here.

Other name(s): AF0464 (gene name); 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor)

Systematic name: 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid:ferredoxin oxidoreductase

Comments: A flavoprotein (FAD). The enzyme is involved in the biosynthesis of archaeal membrane lipids. It catalyses the reduction of all 8 double bonds in 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipids and all 4 double bonds in 3-O-geranylgeranyl-sn-glycerol phospholipids with comparable activity. Unlike EC 1.3.1.101, 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H], this enzyme shows no activity with NADPH, and requires a dedicated ferredoxin [4].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Murakami, M., Shibuya, K., Nakayama, T., Nishino, T., Yoshimura, T. and Hemmi, H. Geranylgeranyl reductase involved in the biosynthesis of archaeal membrane lipids in the hyperthermophilic archaeon Archaeoglobus fulgidus. FEBS J. 274 (2007) 805-814. [PMID: 17288560]

2. Sato, S., Murakami, M., Yoshimura, T. and Hemmi, H. Specific partial reduction of geranylgeranyl diphosphate by an enzyme from the thermoacidophilic archaeon Sulfolobus acidocaldarius yields a reactive prenyl donor, not a dead-end product. J. Bacteriol. 190 (2008) 3923-3929. [PMID: 18375567]

3. Sasaki, D., Fujihashi, M., Iwata, Y., Murakami, M., Yoshimura, T., Hemmi, H. and Miki, K. Structure and mutation analysis of archaeal geranylgeranyl reductase. J. Mol. Biol. 409 (2011) 543-557. [PMID: 21515284]

4. Isobe, K., Ogawa, T., Hirose, K., Yokoi, T., Yoshimura, T. and Hemmi, H. Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells. J. Bacteriol. 196 (2014) 417-423. [PMID: 24214941]

[EC 1.3.7.11 created 2013 as EC 1.3.99.34, transferred 2015 to EC 1.3.7.11]

EC 1.3.7.12

Accepted name: red chlorophyll catabolite reductase

Reaction: primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

For diagram of reaction click here.

Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-8,23-dihydro-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
primary fluorescent chlorophyll catabolite = pFCC = (82R,12S,13S)-12-(2-carboxyethyl)-3-ethyl-1-formyl-82-(methoxycarbonyl)-2,7,13,17-tetramethyl-18-vinyl-12,13-dihydro-8,10-ethanobilene-b-81,19(16H)-dione

Other name(s): RCCR; RCC reductase; red Chl catabolite reductase

Systematic name: primary fluorescent chlorophyll catabolite:ferredoxin oxidoreductase

Comments: The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I [1,2]. This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17, pheophorbide a oxygenase [3]. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer [3,4]. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs) [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669-676. [PMID: 12223835]

2. Wüthrich, K.L., Bovet, L., Hunziker, P.E., Donnison, I.S. and Hörtensteiner, S. Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21 (2000) 189-198. [PMID: 10743659]

3. Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369-387. [PMID: 17237353]

4. Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55-77. [PMID: 16669755]

5. Rodoni, S., Vicentini, F., Schellenberg, M., Matile, P. and Hörtensteiner, S. Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown. Plant Physiol. 115 (1997) 677-682. [PMID: 12223836]

[EC 1.3.7.12 created 2007 as EC 1.3.1.80, transferred 2016 to EC 1.3.7.12]

EC 1.3.7.13

Accepted name: 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin)

Reaction: protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster = 3,8-divinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

For diagram of reaction click here.

Other name(s): bciB (gene name); cyano-type divinyl chlorophyllide a 8-vinyl-reductase

Systematic name: protochlorophyllide-a:ferredoxin C-81-oxidoreductase

Comments: The enzyme, found in many phototrophic bacteria, land plants, and some green and red algae, is involved in the production of monovinyl versions of (bacterio)chlorophyll pigments from their divinyl precursors. Binds two [4Fe-4S] clusters and an FAD cofactor. It can also act on 3,8-divinyl chlorophyllide a, 3,8-divinyl chlorophyll a, and chlorophyll c2. cf. EC 1.3.1.75, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Chew, A.G. and Bryant, D.A. Characterization of a plant-like protochlorophyllide a divinyl reductase in green sulfur bacteria. J. Biol. Chem. 282 (2007) 2967-2975. [PMID: 17148453]

2. Saunders, A.H., Golbeck, J.H. and Bryant, D.A. Characterization of BciB: a ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium. Biochemistry 52 (2013) 8442-8451. [PMID: 24151992]

3. Ito, H. and Tanaka, A. Evolution of a new chlorophyll metabolic pathway driven by the dynamic changes in enzyme promiscuous activity. Plant Cell Physiol 55 (2014) 593-603. [PMID: 24399236]

[EC 1.3.7.13 created 2016]

EC 1.3.7.14

Accepted name: 3,8-divinyl chlorophyllide a reductase

Reaction: bacteriochlorophyllide g + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3,8-divinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+

For diagram of reaction click here.

Systematic name: bacteriochlorophyllide-g:ferredoxin C-81-oxidoreductase

Comments: The enzyme, found only in bacteriochlorophyll b-producing bacteria, catalyses the introduction of a C-8 ethylidene group. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase. It is very similar to EC 1.3.7.15, chlorophyllide a reductase, and is composed of three subunits. Two of them form the catalytic component, while the third one functions as an ATP-dependent reductase component that catalyses the electron transfer from ferredoxin to the catalytic component.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Tsukatani, Y., Yamamoto, H., Harada, J., Yoshitomi, T., Nomata, J., Kasahara, M., Mizoguchi, T., Fujita, Y. and Tamiaki, H. An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light. Sci Rep 3 (2013) 1217. [PMID: 23386973]

2. Tsukatani, Y., Harada, J., Nomata, J., Yamamoto, H., Fujita, Y., Mizoguchi, T. and Tamiaki, H. Rhodobacter sphaeroides mutants overexpressing chlorophyllide a oxidoreductase of Blastochloris viridis elucidate functions of enzymes in late bacteriochlorophyll biosynthetic pathways. Sci Rep 5 (2015) 9741. [PMID: 25978726]

[EC 1.3.7.14 created 2016]

EC 1.3.7.15

Accepted name: chlorophyllide a reductase

Reaction: (1) 3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(2) bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(3) 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+

For diagram of reaction click here.

Other name(s): bchX (gene name); bchY (gene name); bchZ (gene name); COR

Systematic name: bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase

Comments: The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) [4]. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Nomata, J., Mizoguchi, T., Tamiaki, H. and Fujita, Y. A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus. J. Biol. Chem. 281 (2006) 15021-15028. [PMID: 16571720]

2. Tsukatani, Y., Yamamoto, H., Harada, J., Yoshitomi, T., Nomata, J., Kasahara, M., Mizoguchi, T., Fujita, Y. and Tamiaki, H. An unexpectedly branched biosynthetic pathway for bacteriochlorophyll b capable of absorbing near-infrared light. Sci Rep 3 (2013) 1217. [PMID: 23386973]

3. Lange, C., Kiesel, S., Peters, S., Virus, S., Scheer, H., Jahn, D. and Moser, J. Broadened substrate specificity of 3-hydroxyethyl bacteriochlorophyllide a dehydrogenase (BchC) indicates a new route for the biosynthesis of bacteriochlorophyll a. J. Biol. Chem. 290 (2015) 19697-19709. [PMID: 26088139]

4. Harada, J., Mizoguchi, T., Tsukatani, Y., Yokono, M., Tanaka, A. and Tamiaki, H. Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis. J. Biol. Chem. 289 (2014) 12716-12726. [PMID: 24637023]

[EC 1.3.7.15 created 1965 as EC 1.3.99.35, modified 2012, transferred 2016 to EC 1.3.7.15]


EC 1.3.8 With flavin as acceptor

Contents

EC 1.3.8.1 short-chain acyl-CoA dehydrogenase
EC 1.3.8.2 4,4'-diapophytoene desaturase
EC 1.3.8.3 (R)-benzylsuccinyl-CoA dehydrogenase
EC 1.3.8.4 isovaleryl-CoA dehydrogenase
EC 1.3.8.5 2-methyl-branched-chain-enoyl-CoA reductase
EC 1.3.8.6 glutaryl-CoA dehydrogenase (decarboxylating)
EC 1.3.8.7 medium-chain acyl-CoA dehydrogenase
EC 1.3.8.8 long-chain acyl-CoA dehydrogenase
EC 1.3.8.9 very-long-chain acyl-CoA dehydrogenase
EC 1.3.8.10 cyclohex-1-ene-1-carbonyl-CoA dehydrogenase
EC 1.3.8.11 cyclohexane-1-carbonyl-CoA dehydrogenase
EC 1.3.8.12 (2S)-methylsuccinyl-CoA dehydrogenase
EC 1.3.8.13 crotonobetainyl-CoA reductase

EC 1.3.8.1

Accepted name: short-chain acyl-CoA dehydrogenase

Reaction: a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

Glossary: a short-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains less than 6 carbon atoms.

Other name(s): butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name).

Systematic name: short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9027-88-7

References:

1. Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 13-26. [PMID: 13130522]

2. Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M. Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 1-12. [PMID: 13130521]

3. Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447-466.

4. Shaw, L. and Engel, P.C. The purification and properties of ox liver short-chain acyl-CoA dehydrogenase. Biochem. J. 218 (1984) 511-520. [PMID: 6712627]

5. Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718-725. [PMID: 7601336]

6. Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311-1325. [PMID: 3968063]

7. McMahon, B., Gallagher, M.E. and Mayhew, S.G. The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates. FEMS Microbiol. Lett. 250 (2005) 121-127. [PMID: 16024185]

[EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012]

EC 1.3.8.2

Accepted name: 4,4'-diapophytoene desaturase

Reaction: 15-cis-4,4'-diapophytoene + 4 FAD = all-trans-4,4'-diapolycopene + 4 FADH2 (overall reaction)
(1a) 15-cis-4,4'-diapophytoene + FAD = all-trans-4,4'-diapophytofluene + FADH2
(1b) all-trans-4,4'-diapophytofluene + FAD = all-trans-4,4'-diapo-ζ-carotene + FADH2
(1c) all-trans-4,4'-diapo-ζ-carotene + FAD = all-trans-4,4'-diaponeurosporene + FADH2
(1d) all-trans-4,4'-diaponeurosporene + FAD = all-trans-4,4'-diapolycopene + FADH2

For diagram of reaction click here

Other name(s): dehydrosqualene desaturase; CrtN; 4,4'-diapophytoene:FAD oxidoreductase

Systematic name: 15-cis-4,4'-diapophytoene:FAD oxidoreductase

Comments: Typical of Staphylococcus aureus and some other bacteria such as Heliobacillus sp. Responsible for four successive dehydrogenations. In some species it only proceeds as far as all-trans-4,4'-diaponeurosporene.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wieland, B., Feil, C., Gloria-Maercker, E., Thumm, G., Lechner, M., Bravo, J.M., Poralla, K. and Gotz, F. Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus. J. Bacteriol. 176 (1994) 7719-7726. [PMID: 8002598]

2. Raisig, A. and Sandmann, G. 4,4'-diapophytoene desaturase: catalytic properties of an enzyme from the C30 carotenoid pathway of Staphylococcus aureus. J. Bacteriol. 181 (1999) 6184-6187. [PMID: 10498735]

3. Raisig, A. and Sandmann, G. Functional properties of diapophytoene and related desaturases of C30 to C40 carotenoid biosynthetic pathways. Biochim. Biophys. Acta 1533 (2001) 164-170. [PMID: 11566453]

[EC 1.3.8.2 created 2011, modified 2011]

EC 1.3.8.3

Accepted name: (R)-benzylsuccinyl-CoA dehydrogenase

Reaction: (R)-2-benzylsuccinyl-CoA + electron-transfer flavoprotein = (E)-2-benzylidenesuccinyl-CoA + reduced electron-transfer flavoprotein

For diagram of reaction, click here

Other name(s): BbsG; (R)-benzylsuccinyl-CoA:(acceptor) oxidoreductase

Systematic name: (R)-benzylsuccinyl-CoA:electron transfer flavoprotein oxidoreductase

Comments: Requires FAD as prosthetic group. Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity; it is highly specific for (R)-benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA. Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica. Ferricenium ion is an effective artificial electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number:

References:

1. Leutwein, C. and Heider, J. Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and β-oxidation of the first intermediate, (R)-(+)-benzylsuccinate. Microbiology 145 (1999) 3265-3271. [PMID: 10589736]

2. Leutwein, C. and Heider, J. (R)-Benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme of the anaerobic toluene catabolic pathway. Arch. Microbiol. 178 (2002) 517-524. [PMID: 12420174]

[EC 1.3.8.3 created 2003 as EC 1.3.99.21, transferred 2012 to EC 1.3.8.3]

EC 1.3.8.4

Accepted name: isovaleryl-CoA dehydrogenase

Reaction: isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Other name(s): isovaleryl-coenzyme A dehydrogenase; isovaleroyl-coenzyme A dehydrogenase; 3-methylbutanoyl-CoA:(acceptor) oxidoreductase

Systematic name: 3-methylbutanoyl-CoA:electron-transfer flavoprotein oxidoreductase

Comments: Contains FAD as prosthetic group. Pentanoate can act as donor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37274-61-6

References:

1. Bachhawat, B.K., Robinson, W.G. and Coon, M.J. Enzymatic carboxylation of β-hydroxyisovaleryl coenzyme A. J. Biol. Chem. 219 (1956) 539-550. [PMID: 13319276]

2. Ikeda, Y. and Tanaka, K. Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J. Biol. Chem. 258 (1983) 1077-1085. [PMID: 6401713]

3. Tanaka, K., Budd, M.A., Efron, M.L. and Isselbacher, K.J. Isovaleric acidemia: a new genetic defect of leucine metabolism. Proc. Natl. Acad. Sci. USA 56 (1966) 236-242. [PMID: 5229850]

[EC 1.3.8.4 created 1978 as EC 1.3.99.10, modified 1986, transferred 2012 to EC 1.3.8.4]

EC 1.3.8.5

Accepted name: 2-methyl-branched-chain-enoyl-CoA reductase

Reaction: 2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+

Systematic name: 2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase

Comments: A flavoprotein (FAD) from Ascaris suum. The enzyme functions in shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 122320-06-3

References:

1. Komuniecki, R., Fekete, S. and Thissen-Parra, J. Purification and characterization of the 2-methyl branched-chain acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum. J. Biol. Chem. 260 (1985) 4770-4777. [PMID: 3988734]

2. Komuniecki, R., McCrury, J., Thissen, J. and Rubin, N. Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction. Biochim. Biophys. Acta 975 (1989) 127-131. [PMID: 2736251]

[EC 1.3.8.5 created 1992 as EC 1.3.1.52, transferred 2012 to EC 1.3.8.5]

EC 1.3.8.6

Accepted name: glutaryl-CoA dehydrogenase (decarboxylating)

Reaction: glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein (overall reaction)
(1a) glutaryl-CoA + electron-transfer flavoprotein = (E)-glutaconyl-CoA + reduced electron-transfer flavoprotein
(1b) (E)-glutaconyl-CoA = crotonyl-CoA + CO2

For diagram of reaction click here.

Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA
crotonyl-CoA = (E)-but-2-enoyl-CoA

Other name(s): glutaryl coenzyme A dehydrogenase; glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating); glutaryl-CoA dehydrogenase

Systematic name: glutaryl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase (decarboxylating)

Comments: Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 4.1.1.70, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA (EC 1.3.99.32).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 37255-38-2

References:

1. Besrat, A., Polan, C.E. and Henderson, L.M. Mammalian metabolism of glutaric acid. J. Biol. Chem. 244 (1969) 1461-1467. [PMID: 4304226]

2. Hartel, U., Eckel, E., Koch, J., Fuchs, G., Linder, D. and Buckel, W. Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate. Arch. Microbiol. 159 (1993) 174-181. [PMID: 8439237]

3. Dwyer, T.M., Zhang, L., Muller, M., Marrugo, F. and Frerman, F. The functions of the flavin contact residues, αArg249 and βTyr16, in human electron transfer flavoprotein. Biochim. Biophys. Acta 1433 (1999) 139-152. [PMID: 10446367]

4. Rao, K.S., Albro, M., Dwyer, T.M. and Frerman, F.E. Kinetic mechanism of glutaryl-CoA dehydrogenase. Biochemistry 45 (2006) 15853-15861. [PMID: 17176108]

[EC 1.3.8.6 created 1972 as EC 1.3.99.7, transferred 2012 to EC 1.3.8.6, modified 2013]

EC 1.3.8.7

Accepted name: medium-chain acyl-CoA dehydrogenase

Reaction: a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

Glossary: a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms.

Other name(s): fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrogenase (ambiguous); medium-chain acyl-coenzyme A dehydrogenase; acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous); ACADM (gene name).

Systematic name: medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [2]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292-294. [PMID: 13239683]

2. Crane, F.L., Mii, S., Hauge, J.G., Green, D.E. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase. J. Biol. Chem. 218 (1956) 701-716. [PMID: 13295224]

3. Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447-466.

4. Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311-1325. [PMID: 3968063]

5. Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718-725. [PMID: 7601336]

6. Kim, J.J., Wang, M. and Paschke, R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. USA 90 (1993) 7523-7527. [PMID: 8356049]

7. Peterson, K.L., Sergienko, E.E., Wu, Y., Kumar, N.R., Strauss, A.W., Oleson, A.E., Muhonen, W.W., Shabb, J.B. and Srivastava, D.K. Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules. Biochemistry 34 (1995) 14942-14953. [PMID: 7578106]

8. Toogood, H.S., van Thiel, A., Basran, J., Sutcliffe, M.J., Scrutton, N.S. and Leys, D. Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J. Biol. Chem. 279 (2004) 32904-32912. [PMID: 15159392]

[EC 1.3.8.7 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.7]

EC 1.3.8.8

Accepted name: long-chain acyl-CoA dehydrogenase

Reaction: a long-chain acyl-CoA + electron-transfer flavoprotein = a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

Glossary: a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms.

Other name(s): palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name).

Systematic name: long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 59536-74-2

References:

1. Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292-294. [PMID: 13239683]

2. Hauge, J.G., Crane, F.L. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase. J. Biol. Chem. 219 (1956) 727-733. [PMID: 13319294]

3. Hall, C.L., Heijkenkjold, L., Bartfai, T., Ernster, L. and Kamin, H. Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria. Arch. Biochem. Biophys. 177 (1976) 402-414. [PMID: 1015826]

4. Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311-1325. [PMID: 3968063]

5. Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W. and Kim, J.J. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Biochemistry 33 (1994) 4258-4264. [PMID: 8155643]

[EC 1.3.8.8 created 1989 as EC 1.3.99.13, part transferred 2012 to EC 1.3.8.8]

EC 1.3.8.9

Accepted name: very-long-chain acyl-CoA dehydrogenase

Reaction: a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.

Other name(s): ACADVL (gene name).

Systematic name: very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and Hashimoto, T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 1027-1033. [PMID: 1730632]

2. Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K. and Hashimoto, T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest. 95 (1995) 2465-2473. [PMID: 7769092]

3. McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J. and Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 283 (2008) 9435-9443. [PMID: 18227065]

[EC 1.3.8.9 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.9]

EC 1.3.8.10

Accepted name: cyclohex-1-ene-1-carbonyl-CoA dehydrogenase

Reaction: cyclohex-1-ene-1-carbonyl-CoA + electron-transfer flavoprotein = cyclohex-1,5-diene-1-carbonyl-CoA + reduced electron-transfer flavoprotein

Systematic name: cyclohex-1-ene-1-carbonyl-CoA:electron transfer flavoprotein oxidoreductase

Comments: Contains FAD. The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane-1-carboxylate, a byproduct produced by that organism during fermentation of benzoate and crotonate to acetate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kung, J.W., Seifert, J., von Bergen, M. and Boll, M. Cyclohexanecarboxyl-coenzyme A (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus. J. Bacteriol. 195 (2013) 3193-3200. [PMID: 23667239]

[EC 1.3.8.10 created 2013]

EC 1.3.8.11

Accepted name: cyclohexane-1-carbonyl-CoA dehydrogenase

Reaction: cyclohexane-1-carbonyl-CoA + electron-transfer flavoprotein = cyclohex-1-ene-1-carbonyl-CoA + reduced electron-transfer flavoprotein

Systematic name: cyclohexane-1-carbonyl-CoA:electron transfer flavoprotein oxidoreductase

Comments: Contains FAD. The enzyme, characterized from the strict anaerobic bacterium Syntrophus aciditrophicus, is involved in production of cyclohexane-1-carboxylate, a byproduct produced by that organism during fermentation of benzoate and crotonate to acetate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Kung, J.W., Seifert, J., von Bergen, M. and Boll, M. Cyclohexanecarboxyl-coenzyme A (CoA) and cyclohex-1-ene-1-carboxyl-CoA dehydrogenases, two enzymes involved in the fermentation of benzoate and crotonate in Syntrophus aciditrophicus. J. Bacteriol. 195 (2013) 3193-3200. [PMID: 23667239]

[EC 1.3.8.11 created 2013]

EC 1.3.8.12

Accepted name: (2S)-methylsuccinyl-CoA dehydrogenase

Reaction: (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein = 2-methylfumaryl-CoA + reduced electron-transfer flavoprotein

Glossary: 2-methylfumaryl-CoA = (E)-3-carboxy-2-methylprop-2-enoyl-CoA

Other name(s): Mcd

Systematic name: (2S)-methylsuccinyl-CoA:electron-transfer flavoprotein oxidoreductase

Comments: The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. The enzyme contains FAD.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Erb, T.J., Fuchs, G. and Alber, B.E. (2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Mol. Microbiol. 73 (2009) 992-1008. [PMID: 19703103]

[EC 1.3.8.12 created 2015]

EC 1.3.8.13

Accepted name: crotonobetainyl-CoA reductase

Reaction: γ-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein

Glossary: γ-butyrobetainyl-CoA = 4-(trimethylammonio)butanoyl-CoA
crotonobetainyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA

Other name(s): caiA (gene name)

Systematic name: γ-butyrobetainyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

Comments: The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21, L-carnitine CoA-transferase. The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Roth, S., Jung, K., Jung, H., Hommel, R.K. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(–)-carnitine. Antonie Van Leeuwenhoek 65 (1994) 63-69. [PMID: 8060125]

2. Preusser, A., Wagner, U., Elssner, T. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim. Biophys. Acta 1431 (1999) 166-178. [PMID: 10209289]

3. Elssner, T., Hennig, L., Frauendorf, H., Haferburg, D. and Kleber, H.P. Isolation, identification, and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA, compounds involved in carnitine metabolism of E. coli. Biochemistry 39 (2000) 10761-10769. [PMID: 10978161]

4. Walt, A. and Kahn, M.L. The fixA and fixB genes are necessary for anaerobic carnitine reduction in Escherichia coli. J. Bacteriol. 184 (2002) 4044-4047. [PMID: 12081978]

[EC 1.3.8.13 created 2017]


EC 1.3.98 With other, known, acceptors

Contents

EC 1.3.98.1 dihydroorotate dehydrogenase (fumarate)
EC 1.3.98.2 transferred now EC 1.3.4.1
EC 1.3.98.3 coproporphyrinogen dehydrogenase
EC 1.3.98.4 5a,11a-dehydrotetracycline reductase


EC 1.3.98.1

Accepted name: dihydroorotate dehydrogenase (fumarate)

Reaction: (S)-dihydroorotate + fumarate = orotate + succinate

Other name(s): DHOdehase (ambiguous); dihydroorotate dehydrogenase (ambiguous); dihydoorotic acid dehydrogenase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); dihydroorotate oxidase, pyr4 (gene name)

Systematic name: (S)-dihydroorotate:fumarate oxidoreductase

Comments: Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-03-2

References:

1. Björnberg, O., Rowland, P., Larsen, S. and Jensen, K.F. Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry 36 (1997) 16197-16205. [PMID: 9405053]

2. Rowland, P., Björnberg, O., Nielsen, F.S., Jensen, K.F. and Larsen, S. The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function. Protein Sci. 7 (1998) 1269-1279. [PMID: 9655329]

3. Nørager, S., Arent, S., Björnberg, O., Ottosen, M., Lo Leggio, L., Jensen, K.F. and Larsen, S. Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function. J. Biol. Chem. 278 (2003) 28812-28822. [PMID: 12732650]

4. Zameitat, E., Pierik, A.J., Zocher, K. and Löffler, M. Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues. FEMS Yeast Res. 7 (2007) 897-904. [PMID: 17617217]

5. Inaoka, D.K., Sakamoto, K., Shimizu, H., Shiba, T., Kurisu, G., Nara, T., Aoki, T., Kita, K. and Harada, S. Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction. Biochemistry 47 (2008) 10881-10891. [PMID: 18808149]

6. Cheleski, J., Wiggers, H.J., Citadini, A.P., da Costa Filho, A.J., Nonato, M.C. and Montanari, C.A. Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry. Anal. Biochem. 399 (2010) 13-22. [PMID: 19932077]

[EC 1.3.98.1 created 1961 as EC 1.3.3.1, transferred 2011 to EC 1.3.98.1]

[EC 1.3.98.2 Transferred entry: fumarate reductase (CoM/CoB). Now EC 1.3.4.1, fumarate reductase (CoM/CoB) (EC 1.3.98.2 created 2014, deleted 2014)]

EC 1.3.98.3

Accepted name: coproporphyrinogen dehydrogenase

Reaction: coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

For diagram of reaction click here.

Other name(s): oxygen-independent coproporphyrinogen-III oxidase; HemN; coproporphyrinogen III oxidase

Systematic name: coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)

Comments: This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. It occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. This conversion, —·CH-CH2-COO- → —CH=CH2 + CO2 + e- replaces the electron initially used.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Layer, G., Verfürth, K., Mahlitz, E. and Jahn, D. Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J. Biol. Chem. 277 (2002) 34136-34142. [PMID: 12114526]

2. Layer, G., Moser, J., Heinz, D.W., Jahn, D. and Schubert, W.D. Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes. EMBO J. 22 (2003) 6214-6224. [PMID: 14633981]

[EC 1.3.98.3 created 2004 as EC 1.3.99.22, transferred 2016 to EC 1.3.98.3]

EC 1.3.98.4

Accepted name: 5a,11a-dehydrotetracycline reductase

Reaction: tetracycline + oxidized coenzyme F420 = 5a,11a-dehydrotetracycline + reduced coenzyme F420

For diagram of reaction click here.

Other name(s): oxyR (gene name); 12-dehydrotetracycline dehydrogenase; dehydrooxytetracycline dehydrogenase; 12-dehydrotetracycline reductase

Systematic name: tetracycline:coenzyme F420 dehydrogenase

Comments: The enzyme, characterized from the bacteria Streptomyces aureofaciens and Streptomyces rimosus, catalyses the last step in the biosynthesis of the tetracycline antibiotics tetracycline and oxytetracycline.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. McCormick, J.R.D., Hirsch, U., Sjolander, N.O. and Doerschuk, A.P. Cosynthesis of tetracyclines by pairs of Streptomyces aureofaciens mutants. J. Am. Chem. Soc. 82 (1960) 5006-5007.

2. Miller, P.A., Sjolander, N.O., Nalesnyk, S., Arnold, N., Johnson, S., Doerschuk, A.P. and McCormick, J.R.D. Cosynthetic factor I, a factor involved in hydrogen-transfer in Streptomyces aureofaciens. J. Am. Chem. Soc. 82 (1960) 5002-5003.

3. McCormick, J.R.D. and Morton, G.O. Identity of cosynthetic factor I of Streptomyces aureofaciens and fragment FO from coenzyme F420 of Methanobacterium species. J. Am. Chem. Soc. 104 (1982) 4014-4015.

4. Wang, P., Bashiri, G., Gao, X., Sawaya, M.R. and Tang, Y. Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis. J. Am. Chem. Soc. 135 (2013) 7138-7141. [PMID: 23621493]

[EC 1.3.98.4 created 2016]


EC 1.3.99 With other acceptors

Contents

EC 1.3.99.1 deleted, included with EC 1.3.5.1
EC 1.3.99.2 transferred now EC 1.3.8.1
EC 1.3.99.3 transferred now EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9
EC 1.3.99.4 3-oxosteroid 1-dehydrogenase
EC 1.3.99.5 3-oxo-5α-steroid 4-dehydrogenase (acceptor)
EC 1.3.99.6 3-oxo-5β-steroid 4-dehydrogenase
EC 1.3.99.7 transferred now EC 1.3.8.6
EC 1.3.99.8 2-furoyl-CoA dehydrogenase
EC 1.3.99.9 now EC 1.21.99.1
EC 1.3.99.10 transferred now EC 1.3.8.4
EC 1.3.99.11 dihydroorotate dehydrogenase
EC 1.3.99.11 now EC 1.3.5.2
EC 1.3.99.12 2-methylacyl-CoA dehydrogenase
EC 1.3.99.13 transferred now EC 1.3.8.8
EC 1.3.99.14 cyclohexanone dehydrogenase
EC 1.3.99.15 transferred now EC 1.3.7.8
EC 1.3.99.16 isoquinoline 1-oxidoreductase
EC 1.3.99.17 quinoline 2-oxidoreductase
EC 1.3.99.18 quinaldate 4-oxidoreductase
EC 1.3.99.19 quinoline-4-carboxylate 2-oxidoreductase
EC 1.3.99.20 transferred now EC 1.3.7.9
EC 1.3.99.21 transferred now EC 1.3.8.3
EC 1.3.99.22 transferred, now EC 1.3.98.3
EC 1.3.99.23 all-trans-retinol 13,14-reductase
EC 1.3.99.24 2-amino-4-deoxychorismate dehydrogenase
EC 1.3.99.25 carvone reductase
EC 1.3.99.26 all-trans-ζ-carotene desaturase
EC 1.3.99.27 1-hydroxycarotenoid 3,4-desaturase
EC 1.3.99.28 phytoene desaturase (neurosporene-forming)
EC 1.3.99.29 phytoene desaturase (ζ-carotene-forming)
EC 1.3.99.30 phytoene desaturase (3,4-didehydrolycopene-forming)
EC 1.3.99.31 phytoene desaturase (lycopene-forming)
EC 1.3.99.32 glutaryl-CoA dehydrogenase (non-decarboxylating)
EC 1.3.99.33 urocanate reductase
EC 1.3.99.34 transferred now EC 1.3.7.11
EC 1.3.99.35 transferred, now EC 1.3.7.15
EC 1.3.99.36 cypemycin cysteine dehydrogenase (decarboxylating)
EC 1.3.99.37 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase
EC 1.3.99.38 menaquinone-9 β-reductase

[EC 1.3.99.1 Deleted entry: succinate dehydrogenase. The activity is included in EC 1.3.5.1, succinate dehydrogenase (quinone). (EC 1.3.99.1 created 1961, deleted 2013)]

[EC 1.3.99.2 Transferred entry: butyryl-CoA dehydrogenase. Now EC 1.3.8.1, butyryl-CoA dehydrogenase. (EC 1.3.99.2 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, deleted 2011)]

[EC 1.3.99.3 Transferred entry: acyl-CoA dehydrogenase, now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase (EC 1.3.99.3 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, deleted 2012)]

EC 1.3.99.4

Accepted name: 3-oxosteroid 1-dehydrogenase

Reaction: a 3-oxosteroid + acceptor = a 3-oxo-δ1-steroid + reduced acceptor

Other name(s): 3-oxosteroid δ1-dehydrogenase; δ1-dehydrogenase; 3-ketosteroid-1-en-dehydrogenase; 3-ketosteroid-δ1-dehydrogenase; 1-ene-dehydrogenase; 3-oxosteroid:(2,6-dichlorphenolindophenol) δ1-oxidoreductase; 4-en-3-oxosteroid:(acceptor)-1-en-oxido-reductase; δ1-steroid reductase; 3-oxosteroid:(acceptor) δ1-oxidoreductase

Systematic name: 3-oxosteroid:acceptor δ1-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9029-04-3

References:

1. Levy, H.R. and Talalay, P. Bacterial oxidation of steroids. II. Studies on the enzymatic mechanisms of ring A dehydrogenation. J. Biol. Chem. 234 (1959) 2014-2021.

[EC 1.3.99.4 created 1965]

EC 1.3.99.5

Accepted name: 3-oxo-5α-steroid 4-dehydrogenase (acceptor)

Reaction: a 3-oxo-5α-steroid + acceptor = a 3-oxo-Δ4-steroid + reduced acceptor

Other name(s): steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 3-oxo-5α-steroid Δ4-dehydrogenase; steroid Δ4-5α-reductase; Δ4-3-keto steroid 5α-reductase; Δ4-3-oxo steroid reductase; Δ4-3-ketosteroid5α-oxidoreductase; Δ4-3-oxosteroid-5α-reductase; 3-keto-Δ4-steroid-5α-reductase; 5α-reductase; testosterone 5α-reductase; 4-ene-3-ketosteroid-5α-oxidoreductase; Δ4-5α-dehydrogenase; 3-oxo-5α-steroid:(acceptor) Δ4-oxidoreductase; tesI (gene name)

Systematic name: 3-oxo-5α-steroid:acceptor Δ4-oxidoreductase

Comments: A flavoprotein. This bacterial enzyme, characterized from Comamonas testosteroni, is involved in androsterone degradation. cf. EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9036-43-5

References:

1. Levy, H.R. and Talalay, P. Bacterial oxidation of steroids. II. Studies on the enzymatic mechanisms of ring A dehydrogenation. J. Biol. Chem. 234 (1959) 2014-2021. [PMID: 13673006]

2. Florin, C., Kohler, T., Grandguillot, M. and Plesiat, P. Comamonas testosteroni 3-ketosteroid-Δ4(5α)-dehydrogenase: gene and protein characterization. J. Bacteriol. 178 (1996) 3322-3330. [PMID: 8655514]

3. Horinouchi, M., Hayashi, T., Yamamoto, T. and Kudo, T. A new bacterial steroid degradation gene cluster in Comamonas testosteroni TA441 which consists of aromatic-compound degradation genes for seco-steroids and 3-ketosteroid dehydrogenase genes. Appl. Environ. Microbiol. 69 (2003) 4421-4430. [PMID: 12902225]

[EC 1.3.99.5 created 1965, modified 2012]

EC 1.3.99.6

Accepted name: 3-oxo-5β-steroid 4-dehydrogenase

Reaction: a 3-oxo-5β-steroid + acceptor = a 3-oxo-δ4-steroid + reduced acceptor

Other name(s): 3-oxo-5β-steroid:(acceptor) δ4-oxidoreductase

Systematic name: 3-oxo-5β-steroid:acceptor δ4-oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9067-97-4

References:

1. Davidson, S.J. and Talalay, P. Purification and mechanism of action of a steroid δ4-5β-dehydrogenase. J. Biol. Chem. 241 (1966) 906-915. [PMID: 5907467]

[EC 1.3.99.6 created 1972]

[EC 1.3.99.7 Transferred entry: glutaryl-CoA dehydrogenase. Now EC 1.3.8.6, glutaryl-CoA dehydrogenase (EC 1.3.99.7 created 1972, deleted 2012)]

EC 1.3.99.8

Accepted name: 2-furoyl-CoA dehydrogenase

Reaction: 2-furoyl-CoA + H2O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced acceptor

Other name(s): furoyl-CoA hydroxylase; 2-furoyl coenzyme A hydroxylase; 2-furoyl coenzyme A dehydrogenase; 2-furoyl-CoA:(acceptor) 5-oxidoreductase (hydroxylating)

Systematic name: 2-furoyl-CoA:acceptor 5-oxidoreductase (hydroxylating)

Comments: A copper protein. The oxygen atom of the -OH produced is derived from water, not O2; the actual oxidative step is probably dehydrogenation of a hydrated form -CHOH-CH2- to -C(OH)=CH-, which tautomerizes non-enzymically to -CO-CH2-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA. Methylene blue, nitro blue, tetrazolium and a membrane fraction from Pseudomonas putida can act as acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 9068-18-2

References:

1. Kitcher, J.P., Trudgill, P.W. and Rees, J.S. Purification and properties of 2-furoyl-coenzyme A hydroxylase from Pseudomonas putida F2. Biochem. J. 130 (1972) 121-132.

[EC 1.3.99.8 created 1976]

[EC 1.3.99.9 Transferred entry: now EC 1.21.99.1, β-cyclopiazonate dehydrogenase (EC 1.3.99.9 created 1976, deleted 2002)]

[EC 1.3.99.10 Transferred entry: isovaleryl-CoA dehydrogenase. Now EC 1.3.8.4, isovaleryl-CoA dehydrogenase (EC 1.3.99.10 created 1978, modified 1986, deleted 2012)]

[EC 1.3.99.11 Transferred entry: dihydroorotate dehydrogenase. As the acceptor is now known, the enzyme has been transferred to EC 1.3.5.2, dihydroorotate dehydrogenase (EC 1.3.99.11 created 1983, deleted 2009)]

EC 1.3.99.12

Accepted name: 2-methylacyl-CoA dehydrogenase

Reaction: 2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor

Other name(s): branched-chain acyl-CoA dehydrogenase; 2-methyl branched chain acyl-CoA dehydrogenase; 2-methylbutanoyl-CoA:(acceptor) oxidoreductase

Systematic name: 2-methylbutanoyl-CoA:acceptor oxidoreductase

Comments: Also oxidizes 2-methylpropanoyl-CoA. Not identical with EC 1.3.8.1 (butyryl-CoA dehydrogenase), EC 1.3.8.7 (medium-chain acyl-CoA dehydrogenase), EC 1.3.8.8 (long-chain acyl-CoA dehydrogenase), EC 1.3.8.9 (very-long-chain acyl-CoA dehydrogenase) or EC 1.3.99.10 (isovaleryl-CoA dehydrogenase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 85130-32-1

References:

1. Ikeda, Y., Dabrowski, C. and Tanaka, K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase. J. Biol. Chem. 258 (1983) 1066-1076. [PMID: 6401712]

[EC 1.3.99.12 created 1986]

[EC 1.3.99.13 Transferred entry: long-chain-acyl-CoA dehydrogenase. Now EC 1.3.8.8, long-chain-acyl-CoA dehydrogenase (EC 1.3.99.13 created 1989, deleted 2012)]

EC 1.3.99.14

Accepted name: cyclohexanone dehydrogenase

Reaction: cyclohexanone + acceptor = cyclohex-2-enone + reduced acceptor

Other name(s): cyclohexanone:(acceptor) 2-oxidoreductase

Systematic name: cyclohexanone:acceptor 2-oxidoreductase

Comments: 2,6-Dichloroindophenol can act as acceptor. The corresponding ketones of cyclopentane and cycloheptane cannot act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 123516-43-8

References:

1. Dangel, W., Tschech, A. and Fuchs, G. Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species. Arch. Microbiol. 152 (1989) 273-279. [PMID: 2505723]

[EC 1.3.99.14 created 1992]

[EC 1.3.99.15 Transferred entry: benzoyl-CoA reductase. Now EC 1.3.7.8. (EC 1.3.99.15 created 1999, deleted 2011)]

EC 1.3.99.16

Accepted name: isoquinoline 1-oxidoreductase

Reaction: isoquinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced acceptor

Systematic name: isoquinoline:acceptor 1-oxidoreductase (hydroxylating)

Comments: the enzyme from Pseudomonas diminuta is specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline. Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride, nitroblue tetrazolium, Meldola blue and phenazine methosulfate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 155948-73-5

References:

1. Lehmann, M., Tshisuaka, B., Fetzner, S., Roger, P. and Lingens, F. Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase. J. Biol. Chem. 269 (1994) 11254-11260. [PMID: 8157655]

2. Lehmann, M., Tshisuaka, B., Fetzner, S. and Lingens, F. Molecular cloning of the isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases. J. Biol. Chem. 270 (1995) 14420-14429. [PMID: 7782304]

[EC 1.3.99.16 created 1999]

EC 1.3.99.17

Accepted name: quinoline 2-oxidoreductase

Reaction: quinoline + acceptor + H2O = quinolin-2(1H)-one + reduced acceptor

Systematic name: quinoline:acceptor 2-oxidoreductase (hydroxylating)

Comments: Quinolin-2-ol, quinolin-7-ol, quinolin-8-ol, 3-, 4- and 8-methylquinolines and 8-chloroquinoline are substrates. Iodonitrotetrazolium chloride can act as an electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 132264-32-5

References:

1. Bauder, R., Tshisuaka, B. and Lingens, F. Microbial metabolism of quinoline and related compounds. VII. Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 371 (1990) 1137-1144.

2. Tshisuaka, B., Kappl, R., Huttermann, J. and Lingens, F. Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy. Biochemistry 32 (1993) 12928-12934. [PMID: 8251516]

3. Peschke, B. and Lingens, F. Microbial metabolism of quinoline and related compounds. XII. Isolation and characterization of the quinoline oxidoreductase from Rhodococcus sp. B1 compared with the quinoline oxidoreductase from Pseudomonas putida 86. Biol. Chem. Hoppe-Seyler 372 (1991) 1081-1088. [PMID: 1789933]

4. Schach, S., Tshisuaka, B., Fetzner, S. and Lingens, F. Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation. Eur. J. Biochem. 232 (1995) 536-544. [PMID: 7556204]

[EC 1.3.99.17 created 1999]

EC 1.3.99.18

Accepted name: quinaldate 4-oxidoreductase

Reaction: quinaldate + acceptor + H2O = kynurenate + reduced acceptor

Other name(s): quinaldic acid 4-oxidoreductase

Systematic name: quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating)

Comments: the enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes. 2,4,6-Trinitrobenzene sulfonate, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium, thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride, phenazine methosulfate, 2,6-dichlorophenolindophenol and cytochrome c will act as electron acceptors for both.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 149885-77-8

References:

1. Sauter, M., Tshisuaka, B., Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases. Biol. Chem. Hoppe Seyler 374 (1993) 1037-1046. [PMID: 8292263]

2. Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe-Seyler 374 (1993) 363-376. [PMID: 8357532]

[EC 1.3.99.18 created 1999]

EC 1.3.99.19

Accepted name: quinoline-4-carboxylate 2-oxidoreductase

Reaction: quinoline-4-carboxylate + acceptor + H2O = 2-oxo-1,2-dihydroquinoline-4-carboxylate + reduced acceptor

For diagram, click here

Other name(s): quinaldic acid 4-oxidoreductase; quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating)

Systematic name: quinoline-4-carboxylate:acceptor 2-oxidoreductase (hydroxylating)

Comments: A molybdenum—iron—sulfur flavoprotein with molybdopterin cytosine dinucleotide as the molybdenum cofactor. Quinoline, 4-methylquinoline and 4-chloroquinoline can also serve as substrates for the enzyme from Agrobacterium sp. 1B. Iodonitrotetrazolium chloride, thionine, menadione and 2,6-dichlorophenolindophenol can act as electron acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 175780-18-4

References:

1. Bauer, G. and Lingens, F. Microbial metabolism of quinoline and related compounds. XV. Quinoline-4-carboxylic acid oxidoreductase from Agrobacterium spec.1B: a molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 373 (1992) 699-705. [PMID: 1418685]

[EC 1.3.99.19 created 1999, modified 2006]

[EC 1.3.99.20 Transferred entry: EC 1.3.99.20, 4-hydroxybenzoyl-CoA reductase. Now EC 1.3.7.9, 4-hydroxybenzoyl-CoA reductase. (EC 1.3.99.20 created 2000, deleted 2011)]

[EC 1.3.99.21 Transferred entry: (R)-benzylsuccinyl-CoA dehydrogenase. Now EC 1.3.8.3, (R)-benzylsuccinyl-CoA dehydrogenase (EC 1.3.99.21 created 2003 as EC 1.3.99.21, deleted 2012)]

[EC 1.3.99.22 Transferred entry: coproporphyrinogen dehydrogenase. Now EC 1.3.98.3, coproporphyrinogen dehydrogenase (EC 1.3.99.22 created 2004, deleted 2016)]

EC 1.3.99.23

Accepted name: all-trans-retinol 13,14-reductase

Reaction: all-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor

For diagram of reaction click here.

Other name(s): retinol saturase; RetSat; (13,14)-all-trans-retinol saturase; all-trans-retinol:all-trans-13,14-dihydroretinol saturase

Systematic name: all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase

Comments: The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate. Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates. May play a role in the metabolism of vitamin A.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 879291-21-1

References:

1. Moise, A.R., Kuksa, V., Imanishi, Y. and Palczewski, K. Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase. J. Biol. Chem. 279 (2004) 50230-50242. [PMID: 15358783]

[EC 1.3.99.23 created 2005]

EC 1.3.99.24

Accepted name: 2-amino-4-deoxychorismate dehydrogenase

Reaction: (2S)-2-amino-4-deoxychorismate + FMN = 3-(1-carboxyvinyloxy)anthranilate + FMNH2

For diagram of reaction, click here

Glossary: (2S)-2-amino-4-deoxychorismate = (2S,3S)-3-(1-carboxyvinyloxy)-2,3-dihydroanthranilate
3-enolpyruvoylanthranilate = 3-(1-carboxyvinyloxy)anthranilate

Other name(s): ADIC dehydrogenase; 2-amino-2-deoxyisochorismate dehydrogenase; SgcG

Systematic name: (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase

Comments: The sequential action of EC 2.6.1.86, 2-amino-4-deoxychorismate synthase and this enzyme leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Van Lanen, S.G., Lin, S. and Shen, B. Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism. Proc. Natl. Acad. Sci. USA 105 (2008) 494-499. [PMID: 18182490]

2. Yu, L., Mah, S., Otani, T. and Dedon, P. The benzoxazolinate of C-1027 confers intercalative DNA binding. J. Am. Chem. Soc. 117 (1995) 8877-8878.

[EC 1.3.99.24 created 2008]

EC 1.3.99.25

Accepted name: carvone reductase

Reaction: (1) (+)-dihydrocarvone + acceptor = (–)-carvone + reduced acceptor
(2) (–)-isodihydrocarvone + acceptor = (+)-carvone + reduced acceptor

For diagram of reaction click here.

Glossary: (+)-dihydrocarvone = (1S,4R)-menth-8-en-2-one
(+)-isodihydrocarvone = (1S,4R)-menth-8-en-2-one
(–)-carvone = (4R)-mentha-1(6),8-dien-6-one = (5R)-2-methyl-5-(prop-1-en-2-yl)cyclohex-2-en-1-one

Systematic name: (+)-dihydrocarvone:acceptor 1,6-oxidoreductase

Comments: This enzyme participates in the carveol and dihydrocarveol degradation pathway of the Gram-positive bacterium Rhodococcus erythropolis DCL14. The enzyme has not been purified, and requires an unknown cofactor, which is different from NAD+, NADP+ or a flavin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. van der Werf, M.J. and Boot, A.M. Metabolism of carveol and dihydrocarveol in Rhodococcus erythropolis DCL14. Microbiology 146 (2000) 1129-1141. [PMID: 10832640]

[EC 1.3.99.25 created 2008]

EC 1.3.99.26

Accepted name: all-trans-ζ-carotene desaturase

Reaction: all-trans-ζ-carotene + 2 acceptor = all-trans-lycopene + 2 reduced acceptor (overall reaction)
(1a) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
(1b) all-trans-neurosporene + acceptor = all-trans-lycopene + reduced acceptor

For diagram of reaction click here.

Other name(s): Crtlb; phytoene desaturase (ambiguous); 2-step phytoene desaturase (ambiguous); two-step phytoene desaturase (ambiguous); CrtI (ambiguous)

Systematic name: all-trans-ζ-carotene:acceptor oxidoreductase

Comments: This enzyme is involved in carotenoid biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Iniesta, A.A., Cervantes, M. and Murillo, F.J. Cooperation of two carotene desaturases in the production of lycopene in Myxococcus xanthus. FEBS J. 274 (2007) 4306-4314. [PMID: 17662111]

[EC 1.3.99.26 created 2011]

EC 1.3.99.27

Accepted name: 1-hydroxycarotenoid 3,4-desaturase

Reaction: 1-hydroxy-1,2-dihydrolycopene + acceptor = 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor

For diagram of reaction click here or click here

Other name(s): CrtD; hydroxyneurosporene desaturase; carotenoid 3,4-dehydrogenase; 1-hydroxy-carotenoid 3,4-dehydrogenase

Systematic name: 1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase

Comments: The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides prefer the acyclic carotenoids (e.g. 1-hydroxy-1,2-dihydroneurosporene, 1-hydroxy-1,2-dihydrolycopene) as substrates. The conversion rate for the 3,4-desaturation of the monocyclic 1'-hydroxy-1',2'-dihydro-γ-carotene is lower [2,3]. The enzyme from the marine bacterium strain P99-3 shows high activity with the monocyclic carotenoid 1'-hydroxy-1',2'-dihydro-γ-carotene [1]. The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as the electron acceptor in vitro [3]. However, oxygen is unlikely to be the natural electron acceptor under anaerobic conditions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Teramoto, M., Rahlert, N., Misawa, N. and Sandmann, G. 1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol. FEBS Lett. 570 (2004) 184-188. [PMID: 15251462]

2. Steiger, S., Astier, C. and Sandmann, G. Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin. Biochem. J. 349 (2000) 635-640. [PMID: 10880364]

3. Albrecht, M., Ruther, A. and Sandmann, G. Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spheroidene in Rhodobacter sphaeroides. J. Bacteriol. 179 (1997) 7462-7467. [PMID: 9393712]

[EC 1.3.99.27 created 2011]

EC 1.3.99.28

Accepted name: phytoene desaturase (neurosporene-forming)

Reaction: 15-cis-phytoene + 3 acceptor = all-trans-neurosporene + 3 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
(1c) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor

For diagram of reaction click here.

Other name(s): 3-step phytoene desaturase; three-step phytoene desaturase; phytoene desaturase (ambiguous); CrtI (ambiguous)

Systematic name: 15-cis-phytoene:acceptor oxidoreductase (neurosporene-forming)

Comments: This enzyme is involved in carotenoid biosynthesis and catalyses up to three desaturation steps (cf. EC 1.3.99.29 [phytoene desaturase (ζ-carotene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)], EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]). The enzyme is activated by FAD. NAD+, NADP+ or ATP show no activating effect [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Raisig, A., Bartley, G., Scolnik, P. and Sandmann, G. Purification in an active state and properties of the 3-step phytoene desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli. J. Biochem. 119 (1996) 559-564. [PMID: 8830054]

2. Wang, C.W. and Liao, J.C. Alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution. J. Biol. Chem. 276 (2001) 41161-41164. [PMID: 11526111]

[EC 1.3.99.28 created 2011]

EC 1.3.99.29

Accepted name: phytoene desaturase (ζ-carotene-forming)

Reaction: 15-cis-phytoene + 2 acceptor = all-trans-ζ-carotene + 2 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor

For diagram of reaction click here.

Other name(s): CrtIa; 2-step phytoene desaturase (ambiguous); two-step phytoene desaturase (ambiguous)

Systematic name: 15-cis-phytoene:acceptor oxidoreductase (ζ-carotene-forming)

Comments: The enzyme is involved in carotenoid biosynthesis and catalyses up to two desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Iniesta, A.A., Cervantes, M. and Murillo, F.J. Cooperation of two carotene desaturases in the production of lycopene in Myxococcus xanthus. FEBS J. 274 (2007) 4306-4314. [PMID: 17662111]

[EC 1.3.99.29 created 2011]

EC 1.3.99.30

Accepted name: phytoene desaturase (3,4-didehydrolycopene-forming)

Reaction: 15-cis-phytoene + 5 acceptor = all-trans-3,4-didehydrolycopene + 5 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
(1c) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
(1d) all-trans-neurosporene + acceptor = all-trans-lycopene + reduced acceptor
(1e) all-trans-lycopene + acceptor = all-trans-3,4-didehydrolycopene + reduced acceptor

For diagram of reaction click here.

Other name(s): 5-step phytoene desaturase; five-step phytoene desaturase; phytoene desaturase (ambiguous); Al-1

Systematic name: 15-cis-phytoene:acceptor oxidoreductase (3,4-didehydrolycopene-forming)

Comments: This enzyme is involved in carotenoid biosynthesis and catalyses up to five desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.29 [phytoene desaturase (ζ-carotene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hausmann, A. and Sandmann, G. A single five-step desaturase is involved in the carotenoid biosynthesis pathway to β-carotene and torulene in Neurospora crassa. Fungal Genet. Biol. 30 (2000) 147-153. [PMID: 11017770]

2. Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497-1505. [PMID: 18812228]

[EC 1.3.99.30 created 2011]

EC 1.3.99.31

Accepted name: phytoene desaturase (lycopene-forming)

Reaction: 15-cis-phytoene + 4 acceptor = all-trans-lycopene + 4 reduced acceptor (overall reaction)
(1a) 15-cis-phytoene + acceptor = all-trans-phytofluene + reduced acceptor
(1b) all-trans-phytofluene + acceptor = all-trans-ζ-carotene + reduced acceptor
(1c) all-trans-ζ-carotene + acceptor = all-trans-neurosporene + reduced acceptor
(1d) all-trans-neurosporene + acceptor = all-trans-lycopene + reduced acceptor

For diagram of reaction click here.

Other name(s): 4-step phytoene desaturase; four-step phytoene desaturase; phytoene desaturase (ambiguous); CrtI (ambiguous)

Systematic name: 15-cis-phytoene:acceptor oxidoreductase (lycopene-forming)

Comments: Requires FAD. The enzyme is involved in carotenoid biosynthesis and catalyses up to four desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.29 [phytoene desaturase (ζ-carotene-forming)] and EC 1.3.99.30 [phytoene desaturase (3,4-didehydrolycopene-forming)]).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Fraser, P.D., Misawa, N., Linden, H., Yamano, S., Kobayashi, K. and Sandmann, G. Expression in Escherichia coli, purification, and reactivation of the recombinant Erwinia uredovora phytoene desaturase. J. Biol. Chem. 267 (1992) 19891-19895. [PMID: 1400305]

[EC 1.3.99.31 created 2011]

EC 1.3.99.32

Accepted name: glutaryl-CoA dehydrogenase (non-decarboxylating)

Reaction: glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor

Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA

Other name(s): GDHDes; nondecarboxylating glutaryl-coenzyme A dehydrogenase; nondecarboxylating glutaconyl-coenzyme A-forming GDH

Systematic name: glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating)

Comments: The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wischgoll, S., Taubert, M., Peters, F., Jehmlich, N., von Bergen, M. and Boll, M. Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases in the aromatic metabolism of obligately anaerobic bacteria. J. Bacteriol. 191 (2009) 4401-4409. [PMID: 19395484]

2. Wischgoll, S., Demmer, U., Warkentin, E., Gunther, R., Boll, M. and Ermler, U. Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme A dehydrogenases. Biochemistry 49 (2010) 5350-5357. [PMID: 20486657]

[EC 1.3.99.32 created 2012, modified 2013]

EC 1.3.99.33

Accepted name: urocanate reductase

Reaction: dihydrourocanate + acceptor = urocanate + reduced acceptor

For diagram of reaction click here.

Glossary: urocanate = 3-(1H-imidazol-4-yl)prop-2-enoate
dihydrourocanate = 3-(1H-imidazol-4-yl)propanoate

Other name(s): urdA (gene name)

Systematic name: dihydrourocanate:acceptor oxidoreductase

Comments: The enzyme from the bacterium Shewanella oneidensis MR-1 contains a noncovalently-bound FAD and a covalently-bound FMN. It functions as part of an anaerobic electron transfer chain that utilizes urocanate as the terminal electron acceptor. The activity has been demonstrated with the artificial donor reduced methyl viologen.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bogachev, A.V., Bertsova, Y.V., Bloch, D.A. and Verkhovsky, M.I. Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR-1. Mol. Microbiol. 86 (2012) 1452-1463. [PMID: 23078170]

[EC 1.3.99.33 created 2013]

[EC 1.3.99.34 Transferred entry: 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (donor). Now classified as EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase. (EC 1.3.99.34 created 2013, deleted 2015)]

[EC 1.3.99.35 Transferred entry: chlorophyllide a reductase. Now EC 1.3.7.15, chlorophyllide a reductase (EC 1.3.99.35 created 2014, deleted 2016)]

EC 1.3.99.36

Accepted name: cypemycin cysteine dehydrogenase (decarboxylating)

Reaction: cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor = C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor

For diagram of reaction click here.

Glossary: C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide =

Other name(s): cypemycin decarboxylase; CypD

Systematic name: cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys:acceptor oxidoreductase (decarboxylating)

Comments: Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Claesen, J. and Bibb, M. Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides. Proc. Natl. Acad. Sci. USA 107 (2010) 16297-16302. [PMID: 20805503]

[EC 1.3.99.36 created 2014]

EC 1.3.99.37

Accepted name: 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase

Reaction: (1) dihydroisopentenyldehydrorhodopin + acceptor = isopentenyldehydrorhodopin + reduced acceptor
(2) dihydrobisanhydrobacterioruberin + acceptor = bisanhydrobacterioruberin + reduced acceptor

For diagram of reaction click here.

Glossary: bisanhydrobacterioruberin = (2S,2S')-2,2'-bis(3-methylbut-2-en-1-yl)-3,4-didehydro-1,1',2,2'-tetrahydro-ψ,ψ-carotene-1,1'-diol
dihydrobisanhydrobacterioruberin = (2S,2S')-2,2'-bis(3-methylbut-2-en-1-yl)-3,3',4,4'-tetradehydro-1,1',2,2'-tetrahydro-ψ,ψ-carotene-1,1'-diol
dihydroisopentenyldehydrorhodopin = (2S)-2-(3-methylbut-2-en-1-yl)-3,4-didehydro-1,2-dihydro-ψ,ψ-caroten-1-ol
isopentenyldehydrorhodopin = (2S)-2-(3-methylbut-2-en-1-yl)-1,2-dihydro-ψ,ψ-caroten-1-ol

Other name(s): crtD (gene name)

Systematic name: dihydroisopentenyldehydrorhodopin:acceptor 3,4-oxidoreductase

Comments: The enzyme, isolated from the archaeon Haloarcula japonica, is involved in the biosynthesis of the C50 carotenoid bacterioruberin. In this pathway it catalyses the desaturation of the C-3,4 double bond in dihydroisopentenyldehydrorhodopin and the desaturation of the C-3',4' double bond in dihydrobisanhydrobacterioruberin.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yang, Y., Yatsunami, R., Ando, A., Miyoko, N., Fukui, T., Takaichi, S. and Nakamura, S. Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica. J. Bacteriol. 197 (2015) 1614-1623. [PMID: 25712483]

[EC 1.3.99.37 created 2015]

EC 1.3.99.38

Accepted name: menaquinone-9 β-reductase

Reaction: menaquinone-9 + reduced acceptor = β-dihydromenaquinone-9 + acceptor

Glossary: β-dihydromenaquinone-9 = MK-9(II-H2) = 2-methyl-3-[(2E,10E,14E,18E,22E,26E,30E,33E)-3,7,11,15,19,23,27,31,35-nonamethylhexatriaconta-2,10,14,18,22,26,30,33-octaen-1-yl]naphthalene-1,4-dione

Other name(s): MenJ

Systematic name: menaquinone-9 oxidoreductase (β-dihydromenaquinone-9-forming)

Comments: The enzyme from the bacterium Mycobacterium tuberculosis reduces the β-isoprene unit of menaquinone-9, forming the predominant form of menaquinone found in mycobacteria. Contains FAD.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Upadhyay, A., Fontes, F.L., Gonzalez-Juarrero, M., McNeil, M.R., Crans, D.C., Jackson, M. and Crick, D.C. Partial saturation of menaquinone in Mycobacterium tuberculosis: function and essentiality of a novel reductase, MenJ. ACS Cent. Sci. 1 (2015) 292-302. [PMID: 26436137]

[EC 1.3.99.38 created 2017]


Continued with EC 1.4
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