Enzyme Nomenclature

Continued from EC 1.4

EC 1.5

ACTING ON THE CH-NH GROUP OF DONORS

Sections

EC 1.5.1 With NAD+ or NADP+ as acceptor
EC 1.5.3 With oxygen as acceptor
EC 1.5.4 With a disulfide as acceptor
EC 1.5.5 With a quinone or similar compound as acceptor
EC 1.5.7 With an iron-sulfur protein as acceptor
EC 1.5.8 With a flavin as acceptor
EC 1.5.98 With other, known, physiological acceptor

EC 1.5.99 With unknown physiological acceptor


EC 1.5.1 With NAD+ or NADP+ as acceptor

Contents

EC 1.5.1.1 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]
EC 1.5.1.2 pyrroline-5-carboxylate reductase
EC 1.5.1.3 dihydrofolate reductase
EC 1.5.1.4 deleted, included in EC 1.5.1.3
EC 1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP+)
EC 1.5.1.6 formyltetrahydrofolate dehydrogenase
EC 1.5.1.7 saccharopine dehydrogenase (NAD+, L-lysine-forming)
EC 1.5.1.8 saccharopine dehydrogenase (NADP+, L-lysine-forming)
EC 1.5.1.9 saccharopine dehydrogenase (NAD+, L-glutamate-forming)
EC 1.5.1.10 saccharopine dehydrogenase (NADP+, L-glutamate-forming)
EC 1.5.1.11 D-octopine dehydrogenase
EC 1.5.1.12 transferred now EC 1.2.1.88
EC 1.5.1.13 now EC 1.17.1.5
EC 1.5.1.14 deleted, included in EC 1.5.1.21
EC 1.5.1.15 methylenetetrahydrofolate dehydrogenase (NAD+)
EC 1.5.1.16 D-lysopine dehydrogenase
EC 1.5.1.17 alanopine dehydrogenase
EC 1.5.1.18 ephedrine dehydrogenase
EC 1.5.1.19 D-nopaline dehydrogenase
EC 1.5.1.20 methylenetetrahydrofolate reductase [NAD(P)H]
EC 1.5.1.21 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)
EC 1.5.1.22 strombine dehydrogenase
EC 1.5.1.23 tauropine dehydrogenase
EC 1.5.1.24 N5-(carboxyethyl)ornithine synthase
EC 1.5.1.25 thiomorpholine-carboxylate dehydrogenase
EC 1.5.1.26 β-alanopine dehydrogenase
EC 1.5.1.27 1,2-dehydroreticulinium reductase (NADPH)
EC 1.5.1.28 opine dehydrogenase
EC 1.5.1.29 deleted, now covered by EC 1.5.1.38, EC 1.5.1.39 and EC 1.5.1.41
EC 1.5.1.30 flavin reductase (NADPH)
EC 1.5.1.31 berberine reductase
EC 1.5.1.32 vomilenine reductase
EC 1.5.1.33 pteridine reductase
EC 1.5.1.34 6,7-dihydropteridine reductase
EC 1.5.1.35 deleted, same as EC 1.2.1.19
EC 1.5.1.36 flavin reductase (NADH)
EC 1.5.1.37 FAD reductase (NADH)
EC 1.5.1.38 FMN reductase (NADPH)
EC 1.5.1.39 FMN reductase [NAD(P)H]
EC 1.5.1.40 8-hydroxy-5-deazaflavin:NADPH oxidoreductase
EC 1.5.1.41 riboflavin reductase [NAD(P)H]
EC 1.5.1.42 FMN reductase (NADH)
EC 1.5.1.43 carboxynorspermidine synthase
EC 1.5.1.44 festuclavine dehydrogenase
EC 1.5.1.45 FAD reductase [NAD(P)H]
EC 1.5.1.46 agroclavine dehydrogenase
EC 1.5.1.47 dihydromethanopterin reductase [NAD(P)+]
EC 1.5.1.48 2-methyl-1-pyrroline reductase
EC 1.5.1.49 1-pyrroline-2-carboxylate reductase [NAD(P)H]
EC 1.5.1.50 dihydromonapterin reductase
EC 1.5.1.51 N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase

EC 1.5.1.1

Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]

Reaction: (1) L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+
(2) L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+

Other name(s): Δ1-pyrroline-2-carboxylate reductase; DELTA1-pyrroline-2-carboxylate reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); AbLhpI; pyrroline-2-carboxylate reductase; L-proline:NAD(P)+ 2-oxidoreductase

Systematic name: L-pipecolate/L-proline:NAD(P)+ 2-oxidoreductase

Comments: The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-16-7

References:

1. Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789-800. [PMID: 13502341]

2. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]

[EC 1.5.1.1 created 1961, modified 2015]

EC 1.5.1.2

Accepted name: pyrroline-5-carboxylate reductase

Reaction: L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+

For diagram click here.

Other name(s): proline oxidase; L-proline oxidase; 1-pyrroline-5-carboxylate reductase; NADPH-L1-pyrroline carboxylic acid reductase; L-proline-NAD(P)+ 5-oxidoreductase

Systematic name: L-proline:NAD(P)+ 5-oxidoreductase

Comments: Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-17-8

References:

1. Adams, E. and Goldstone, A. Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3499-3503.

2. Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789-800.

3. Smith, M.E. and Greenberg, D.M. Characterization of an enzyme reducing pyrroline-5-carboxylate to proline. Nature (Lond.) 177 (1956) 1130.

4. Yura, T. and Vogel, H.J. Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties. J. Biol. Chem. 234 (1959) 335-338.

[EC 1.5.1.2 created 1961]

EC 1.5.1.3

Accepted name: dihydrofolate reductase

Reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+

For diagram of reaction click here.

Other name(s): tetrahydrofolate dehydrogenase; DHFR; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; folic acid reductase; folic reductase; dihydrofolic acid reductase; dihydrofolic reductase; 7,8-dihydrofolate reductase; NADPH-dihydrofolate reductase

Systematic name: 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase

Comments: The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9002-03-3

References:

1. Blakley, R.L. and MacDougall, B.M. Dihydrofolic reductase from Streptococcus faecalis R. J. Biol. Chem. 236 (1961) 1163.

2. Bolin, J.T., Filman, D.J., Matthews, D.A. and Kraut, J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257 (1982) 13650-13662. [PMID: 6815178]

3. Kaufman, B.T. and Gardiner, R.C. Studies on dihydrofolic reductase. I. Purification and properties of dihydrofolic reductase from chicken liver. J. Biol. Chem. 241 (1966) 1319-1328. [PMID: 4379915]

4. Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401-411. [PMID: 4306838]

[EC 1.5.1.3 created 1961, modified 1976 (EC 1.5.1.4 created 1961, incorporated 1976)]

[EC 1.5.1.4 Deleted entry: dihydrofolate dehydrogenase. Now included with EC 1.5.1.3 dihydrofolate reductase (EC 1.5.1.4 created 1961, deleted 1976)]

EC 1.5.1.5

Accepted name: methylenetetrahydrofolate dehydrogenase (NADP+)

Reaction: 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH + H+

For diagram of reaction click here (another example).

Other name(s): N5,N10-methylenetetrahydrofolate dehydrogenase; 5,10-methylenetetrahydrofolate:NADP oxidoreductase; 5,10-methylenetetrahydrofolate dehydrogenase; methylenetetrahydrofolate dehydrogenase

Systematic name: 5,10-methylenetetrahydrofolate:NADP+ oxidoreductase

Comments: In eukaryotes, occurs as a trifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and formate—tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes occurs as a bifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-14-5

References:

1. Hatefi, Y., Osborn, M.J., Kay, L.D. and Huennekens, F.M. Hydroxymethyl tetrahydrofolic dehydrogenase. J. Biol. Chem. 227 (1957) 637-647.

2. Osborn, M.J. and Huennekens, F.M. Participation of anhydroleucovorin in the hydroxymethyl tetrahydrofolic dehydrogenase system. Biochim. Biophys. Acta 26 (1957) 646-647.

3. Ramasastri, B.V. and Blakley, R.L. 5,10-Methylenetetrahydrofolic acid dehydrogenase from Bakers' yeast. I. Partial purification and some properties. J. Biol. Chem. 237 (1962) 1982-1988.

4. Yeh, Y.-C. and Greenberg, D.M. Purification and properties of N5,N10-methylenetetrahydrofolate dehydrogenase of calf thymus. Biochim. Biophys. Acta 105 (1965) 279-291. [PMID: 4379024]

[EC 1.5.1.5 created 1961]

EC 1.5.1.6

Accepted name: formyltetrahydrofolate dehydrogenase

Reaction: 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+

For diagram of reaction click here (another example).

Other name(s): 10-formyl tetrahydrofolate:NADP oxidoreductase; 10-formyl-H2PtGlu:NADP oxidoreductase ; 10-formyl-H4folate dehydrogenase; N10-formyltetrahydrofolate dehydrogenase ; 10-formyltetrahydrofolate dehydrogenase

Systematic name: 10-formyltetrahydrofolate:NADP+ oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-25-0

References:

1. Kutzbach, C. and Stokstad, E.L.R. Partial purification of a 10-formyl-tetrahydrofolate: NADP oxidoreductase from mammalian liver. Biochem. Biophys. Res. Commun. 30 (1968) 111-117. [PMID: 4384443]

[EC 1.5.1.6 created 1972]

EC 1.5.1.7

Accepted name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+

For diagram click here, another example.

Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine

Other name(s): lysine—2-oxoglutarate reductase; dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming); ε-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming); N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming)

Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9073-96-5

References:

1. Fujioka, M. and Nakatani, Y. Saccharopine dehydrogenase. Interaction with substrate analogues. Eur. J. Biochem. 25 (1972) 301-307. [PMID: 4339117]

2. Saunders, P.P. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase. J. Biol. Chem. 241 (1966) 3435-3440. [PMID: 4287986]

[EC 1.5.1.7 created 1972]

EC 1.5.1.8

Accepted name: saccharopine dehydrogenase (NADP+, L-lysine-forming)

Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH + H+

For diagram click here.

Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine

Other name(s): lysine-2-oxoglutarate reductase; lysine-ketoglutarate reductase; L-lysine-α-ketoglutarate reductase; lysine:α-ketoglutarate:TPNH oxidoreductase (ε-N-[glutaryl-2]-L-lysine forming); saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase

Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9031-19-0

References:

1. Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62-69. [PMID: 4385118]

2. Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643-11646. [PMID: 6434529]

[EC 1.5.1.8 created 1972]

EC 1.5.1.9

Accepted name: saccharopine dehydrogenase (NAD+, L-glutamate-forming)

Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+

For diagram click here.

Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

Other name(s): dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; saccharopine dehydrogenase (NAD, L-glutamate-forming)

Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming)

(b>Comments: The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-26-1

References:

1. Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62-69. [PMID: 4385118]

2. Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643-11646. [PMID: 6434529]

[EC 1.5.1.9 created 1972]

EC 1.5.1.10

Accepted name: saccharopine dehydrogenase (NADP+, L-glutamate-forming)

Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+

For diagram click here, another example.

Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

Other name(s): saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase

Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-55-0

References:

1. Jones, E.E. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase. J. Biol. Chem. 241 (1966) 3430-3434. [PMID: 4380448]

[EC 1.5.1.10 created 1972]

EC 1.5.1.11

Accepted name: D-octopine dehydrogenase

Reaction: N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+

Other name(s): D-octopine synthase; octopine dehydrogenase; octopine:NAD oxidoreductase; ODH

Systematic name: N2-(D-1-carboxyethyl)-L-arginine:NAD+ oxidoreductase (L-arginine-forming)

Comments: In the reverse direction, acts also on L-ornithine, L-lysine and L-histidine.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 37256-27-2

References:

1. Kemp, J.D., Hack, E., Sutton, D.W. and El-Wakil, M. Unusual amino acids and their relationship to tumorigenesis. Proc. Int. Conf. Plant Pathol. Bact. 4th, (1979) 183-188.

2. van Thoai, N., Huc, C., Pho, D.B. and Olomucki, A. Octopine déhydrogénase. Purification et propriétés catalytiques. Biochim. Biophys. Acta 191 (1969) 46-57. [PMID: 4310628]

[EC 1.5.1.11 created 1972]

[EC 1.5.1.12 Transferred entry: 1-pyrroline-5-carboxylate dehydrogenase. Now EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. (EC 1.5.1.12 created 1972, modified 2008, deleted 2013)]

[EC 1.5.1.13 Transferred entry: now EC 1.17.1.5, nicotinate dehydrogenase. The enzyme was incorrectly classified as acting on a CH-NH group. (EC 1.5.1.13 created 1972, deleted 2004)].

[EC 1.5.1.14 Deleted entry: 1,2-didehydropipecolate reductase. Now included with EC 1.5.1.21 δ1-piperideine-2-carboxylate reductase (EC 1.5.1.14 created 1976, deleted 1989)]

EC 1.5.1.15

Accepted name: methylenetetrahydrofolate dehydrogenase (NAD+)

Reaction: 5,10-methylenetetrahydrofolate + NAD+ = 5,10-methenyltetrahydrofolate + NADH + H+

For diagram of reaction click here.

Other name(s): methylenetetrahydrofolate dehydrogenase (NAD)

Systematic name: 5,10-methylenetetrahydrofolate:NAD+ oxidoreductase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 82062-90-6

References:

1. Moore, M.R., O'Brien, W.E. and Ljungdahl, L.G. Purification and characterization of nicotinamide adenine dinucleotide-dependent methylenetetrahydrofolate dehydrogenase from Clostridium formicoaceticum. J. Biol. Chem. 249 (1974) 5250-5253. [PMID: 4153026]

[EC 1.5.1.15 created 1978]

EC 1.5.1.16

Accepted name: D-lysopine dehydrogenase

Reaction: N2-(D-1-carboxyethyl)-L-lysine + NADP+ + H2O = L-lysine + pyruvate + NADPH + H+

Other name(s): D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase

Systematic name: N2-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)

Comments: In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65187-41-9

References:

1. Otten, L.A.B.M., Vreugdenhil, D. and Schilperoort, R.A. Properties of D(+)-lysopine dehydrogenase from crown gall tumour tissue. Biochim. Biophys. Acta 485 (1977) 268-277. [PMID: 21695]

[EC 1.5.1.16 created 1978]

EC 1.5.1.17

Accepted name: alanopine dehydrogenase

Reaction: 2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+

Other name(s): ALPDH ; alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH; alanopine:NAD oxidoreductase

Systematic name: 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)

Comments: In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 71343-07-2

References:

1. Dando, P.R. Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L. Biochem. Soc. Trans. 9 (1981) 297-298.

2. Fields, J.H.A., Eng, A.K., Ramsden, W.D., Hochachka, P.W. and Weinstein, B. Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas. Arch. Biochem. Biophys. 201 (1980) 110-114. [PMID: 6156653]

3. Fields, J.H.A. and Hochachka, P.W. Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia). Eur. J. Biochem. 114 (1981) 615-621. [PMID: 7238503]

[EC 1.5.1.17 created 1983, modified 1986]

EC 1.5.1.18

Accepted name: ephedrine dehydrogenase

Reaction: (–)-ephedrine + NAD+ = (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+

Systematic name: (–)-ephedrine:NAD+ 2-oxidoreductase

Comments: The product immediately hydrolyses to methylamine and 1-hydroxy-1-phenylpropan-2-one. Acts on a number of related compounds including (–)-sympatol, (+)-pseudoephedrine and (+)-norephedrine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 73508-06-2

References:

1. Klamann, E. and Lingens, F. Degradation of (–)-ephedrine by Pseudomonas putida. Detection of (–)-ephedrine: NAD+-oxidoreductase from Arthrobacter globiformis. Z. Naturforsch. C: Biosci. 35 (1980) 80-87. [PMID: 7405363]

[EC 1.5.1.18 created 1984]

EC 1.5.1.19

Accepted name: D-nopaline dehydrogenase

Reaction: N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O = L-arginine + 2-oxoglutarate + NADPH + H+

Other name(s): D-nopaline synthase; nopaline dehydrogenase; nopaline synthase; NOS

Systematic name: N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)

Comments: In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 64763-57-1

References:

1. Kemp, J.D., Sutton, D.W. and Hack, E. Purification and characterization of the crown gall specific enzyme nopaline synthase. Biochemistry 18 (1979) 3755-3760. [PMID: 476084]

[EC 1.5.1.19 created 1984]

EC 1.5.1.20

Accepted name: methylenetetrahydrofolate reductase [NAD(P)H]

Reaction: 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+

For diagram of reaction click here and for its place in C1 metabolism, click here

Other name(s): methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase; 5,10-methylenetetrahydrofolate reductase (NADPH); 5,10-methylenetetrahydrofolic acid reductase; 5,10-CH2-H4folate reductase; methylenetetrahydrofolate reductase (NADPH2); 5-methyltetrahydrofolate:NAD oxidoreductase; 5-methyltetrahydrofolate:NAD+ oxidoreductase; methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase; 5,10-methylenetetrahydrofolate reductase; methylenetetrahydrofolate reductase; N5,10-methylenetetrahydrofolate reductase; 5,10-methylenetetrahydropteroylglutamate reductase; N5,N10-methylenetetrahydrofolate reductase; methylenetetrahydrofolic acid reductase; 5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect); 5,10-methylenetetrahydrofolate reductase (FADH2); MetF; methylenetetrahydrofolate reductase (NADPH); 5-methyltetrahydrofolate:NADP+ oxidoreductase

Systematic name: 5-methyltetrahydrofolate:NAD(P)+ oxidoreductase

Comments: A flavoprotein (FAD). Menadione can also serve as an electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 71822-25-8

References:

1. Daubner, S.C. and Matthews, R.T. Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem. 257 (1982) 140-145. [PMID: 6975779]

2. Kutzbach, C. and Stokstad, E.L.R. Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta 250 (1971) 459-477. [PMID: 4399897]

3. Sheppard, C.A., Trimmer, E.E. and Matthews, R.G. Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli. J. Bacteriol. 181 (1999) 718-725. [PMID: 9922232]

4. Guenther, B.D., Sheppard, C.A., Tran, P., Rozen, R., Matthews, R.G. and Ludwig, M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 6 (1999) 359-365. [PMID: 10201405]

[EC 1.5.1.20 created 1978 as EC 1.1.1.171, transferred 1984 to EC 1.5.1.20 (EC 1.7.99.5 incorporated 2005), modified 2005]

EC 1.5.1.21

Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)

Reaction: (1) L-pipecolate + NADP+ = 1-piperideine-2-carboxylate + NADPH + H+
(2) L-proline + NADP+ = 1-pyrroline-2-carboxylate + NADPH + H+

Glossary: 1-piperideine-2-carboxylate = 3,4,5,6-tetrahydropyridine-2-carboxylate

Other name(s): Pyr2C reductase; 1,2-didehydropipecolate reductase; P2C reductase; 1,2-didehydropipecolic reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); L-pipecolate:NADP+ 2-oxidoreductase; DELTA1-piperideine-2-carboxylate reductase; Δ1-piperideine-2-carboxylate reductase

Systematic name: L-pipecolate/L-proline:NADP+ 2-oxidoreductase

Comments: The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 52037-88-4

References:

1. Payton, C.W. and Chang, Y.-F. Δ1-Piperideine-2-carboxylate reductase of Pseudomonas putida. J. Bacteriol. 149 (1982) 864-871. [PMID: 6801013]

2. Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. and Esaki, N. The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. J. Biol. Chem. 280 (2005) 5329-5335. [PMID: 15561717]

3. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]

[EC 1.5.1.21 created 1984 (EC 1.5.1.14 created 1976, incorporated 1989), modified 2015]

EC 1.5.1.22

Accepted name: strombine dehydrogenase

Reaction: N-(carboxymethyl)-D-alanine + NAD+ + H2O = glycine + pyruvate + NADH + H+

Other name(s): strombine[N-(carboxymethyl)-D-alanine]dehydrogenase; N-(carboxymethyl)-D-alanine: NAD+ oxidoreductase

Systematic name: N-(carboxymethyl)-D-alanine:NAD+ oxidoreductase (glycine-forming)

Comments: Also catalyses the reaction of EC 1.5.1.17 alanopine dehydrogenase, but more slowly. Does not act on L-strombine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 79393-84-3

References:

1. Dando, P.R. Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine dehydrogenase from the mussel Mytilus edulis L. Biochem. Soc. Trans. 9 (1981) 297-298.

[EC 1.5.1.22 created 1986]

EC 1.5.1.23

Accepted name: tauropine dehydrogenase

Reaction: tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+

Systematic name: N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)

Comments: In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 104645-74-1

References:

1. Gäde, G. Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa. Eur. J. Biochem. 160 (1986) 311-318. [PMID: 3769931]

[EC 1.5.1.23 created 1989]

EC 1.5.1.24

Accepted name: N5-(carboxyethyl)ornithine synthase

Reaction: N5-(L-1-carboxyethyl)-L-ornithine + NADP+ + H2O = L-ornithine + pyruvate + NADPH + H+

Systematic name: N5-(L-1-carboxyethyl)-L-ornithine:NADP+ oxidoreductase (L-ornithine-forming)

Comments: In the reverse direction, L-lysine can act instead of L-ornithine, but more slowly. Acts on the amino group. cf. EC 1.5.1.16 D-lysopine dehydrogenase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129070-70-8

References:

1. Thompson, J. N5-(L-1-Carboxyethyl)-L-ornithine:NADP+ oxidoreductase from Streptococcus lactis. Purification and partial characterization. J. Biol. Chem. 264 (1989) 9592-9601. [PMID: 2498334]

[EC 1.5.1.24 created 1990]

EC 1.5.1.25

Accepted name: thiomorpholine-carboxylate dehydrogenase

Reaction: thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): ketimine reductase; ketimine-reducing enzyme

Systematic name: thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase

Comments: The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 115232-54-7

References:

1. Nardini, M., Ricci, G., Caccuri, A.M., Solinas, S.P., Vesci, L. and Cavallini, D. Purification and characterization of a ketimine-reducing enzyme. Eur. J. Biochem. 173 (1988) 689-694. [PMID: 3371353]

[EC 1.5.1.25 created 1990]

EC 1.5.1.26

Accepted name: β-alanopine dehydrogenase

Reaction: β-alanopine + NAD+ + H2O = β-alanine + pyruvate + NADH + H+

Systematic name: N-(D-1-carboxyethyl)-β-alanine:NAD+ oxidoreductase (β-alanine-forming)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 113573-64-1

References:

1. Sato, M., Takahara, M., Kanno, N., Sato, Y. and Ellington, W.R. Isolation of a new opine, β-alanopine, from the extracts of the muscle of the marine bivalve mollusc Scapharca broughtonii. Comp. Biochem. Physiol. 88B (1987) 803-806.

[EC 1.5.1.26 created 1990]

EC 1.5.1.27

Accepted name: 1,2-dehydroreticulinium reductase (NADPH)

Reaction: (R)-reticuline + NADP+ = 1,2-dehydroreticulinium + NADPH + H+

For diagram click here.

Other name(s): 1,2-dehydroreticulinium ion reductase

Systematic name: (R)-reticuline:NADP+ oxidoreductase

Comments: Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant. The enzyme does not catalyse the reverse reaction to any significant extent under physiological conditions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 130590-58-8

References:

1. De-Eknamkul, W. and Zenk, M.H. Purification and properties of 1,2-dehydroreticulinium reductase from Papaver somniferum seedlings. Phytochemistry 31 (1992) 813-821.

[EC 1.5.1.27 created 1999, modified 2004]

EC 1.5.1.28

Accepted name: opine dehydrogenase

Reaction: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH + H+

Other name(s): (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming)

Systematic name: (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming)

Comments: in the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 108281-02-3

References:

1. Asano, Y., Yamaguchi, K. and Kondo, K. A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C. J. Bacteriol. 171 (1989) 4466-4471. [PMID: 2753861]

2. Dairi, T. and Asano, Y. Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C. Appl. Environ. Microbiol. 61 (1995) 3169-3171. [PMID: 7487048]

3. Kato, Y., Yamada, H. and Asano, Y. Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes. J. Mol. Catal., B Enzym. 1 (1996) 151-160.

[EC 1.5.1.28 created 1999]

[EC 1.5.1.29 Deleted entry: FMN reductase [NAD(P)H]. Now covered by EC 1.5.1.38 [FMN reductase (NADPH)], EC 1.5.1.39 [FMN reductase [NAD(P)H])] and EC 1.5.1.41 (riboflavin reductase [NAD(P)H]) (EC 1.5.1.29 created 1981 as EC 1.6.8.1, transferred 2002 to EC 1.5.1.29, modified 2002, deleted 2011)]

EC 1.5.1.30

Accepted name: flavin reductase (NADPH)

Reaction: reduced riboflavin + NADP+ = riboflavin + NADPH + H+

Other name(s): NADPH:flavin oxidoreductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide phosphate) reductase; flavin mononucleotide reductase; flavine mononucleotide reductase; FMN reductase (NADPH); NADPH-dependent FMN reductase; NADPH-flavin reductase; NADPH-FMN reductase; NADPH-specific FMN reductase; riboflavin mononucleotide reductase; riboflavine mononucleotide reductase; NADPH2 dehydrogenase (flavin); NADPH2:riboflavin oxidoreductase

Systematic name: reduced-riboflavin:NADP+ oxidoreductase

Comments: The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD. NADH is oxidized more slowly than NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56626-29-0

References:

1. Lo, H.-S. and Reeves, R.E. Purification and properties of NADPH:flavin oxidoreductase from Entamoeba histolytica. Mol. Biochem. Parasitol. 2 (1980) 23-30. [PMID: 6258069]

2. Yubisui, T., Tamura, M. and Takeshita, M. Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes. Biochem. Int. 15 (1987) 1-8. [PMID: 3453680]

[EC 1.5.1.30 created 1982 as EC 1.6.8.2, transferred 2002 to EC 1.5.1.30, modified 2011]

EC 1.5.1.31

Accepted name: berberine reductase

Reaction: (R)-canadine + 2 NADP+ = berberine + 2 NADPH + H+

For diagram click here.

Other name(s): (R)-canadine synthase

Systematic name: (R)-tetrahydroberberine:NADP+ oxidoreductase

Comments: Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8 tetrahydroberberine oxidase). Also acts on 7,8-dihydroberberine.

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

References:

1. Bauer, W. and Zenk, M.H. Formation of (R)-configurated tetrahydroprotoberberine alkaloids in vivo and in vitro. Tetrahedron Lett. 32 (1991) 487-490.

[EC 1.5.1.31 created 2002]

EC 1.5.1.32

Accepted name: vomilenine reductase

Reaction: 1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+

For diagram click here.

Systematic name: 1,2-dihydrovomilenine:NADP+ oxidoreductase

Comments: Forms part of the ajmaline biosynthesis pathway.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 462127-03-3

References:

1. von Schumann, G., Gao, S. and Stöckigt, J. Vomilenine reductase - a novel enzyme catalyzing a crucial step in the biosynthesis of the therapeutically applied antiarrhythmic alkaloid ajmaline. J. Bioorg. Med. Chem. 10 (2002) 1913-1918. [PMID: 11937349]

[EC 1.5.1.32 created 2002]

EC 1.5.1.33

Accepted name: pteridine reductase

Reaction: 5,6,7,8-tetrahydrobiopterin + 2 NADP+ = biopterin + 2 NADPH + 2 H+

Other name(s): PTR1; pteridine reductase 1

Systematic name: 5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase

Comments: The enzyme from Leishmania (both amastigote and promastigote forms) catalyses the reduction by NADPH of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to EC 1.5.1.3 (dihydrofolate reductase) and EC 1.5.1.34 (6,7-dihydropteridine reductase), pteridine reductase will not catalyse the reduction of the quinonoid form of dihydrobiopterin. The enzyme is specific for NADPH; no activity has been detected with NADH. It also differs from EC 1.5.1.3 (dihydrofolate reductase) in being specific for the B side of NADPH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 131384-61-7

References:

1. Nare, B., Hardy, L. and Beverley, S.M. The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J. Biol. Chem. 272 (1997) 13883-13891. [PMID: 9153248]

2. Gourley, D.G., Schüttelkopf, A.W., Leonard, G.A., Luba, J., Hardy, L.W., Beverley, S.M. and Hunter, W.N. Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites. Nat. Struct. Biol. 8 (2001) 521-525. [PMID: 11373620]

3. Fitzpatrick, P.F. The aromatic amino acid hydroxylases. Adv. Enzymol. Relat. Areas Mol. Biol. 74 (2000) 235-294. [PMID: 10800597]

[EC 1.5.1.33 created 1999 as EC 1.1.1.253, transferred 2003 to EC 1.5.1.33]

EC 1.5.1.34

Accepted name: 6,7-dihydropteridine reductase

Reaction: a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+

For diagram click here.

Other name(s): 6,7-dihydropteridine:NAD(P)H oxidoreductase; DHPR; NAD(P)H2:6,7-dihydropteridine oxidoreductase; NADH-dihydropteridine reductase; NADPH-dihydropteridine reductase; NADPH-specific dihydropteridine reductase; dihydropteridine (reduced nicotinamide adenine dinucleotide) reductase; dihydropteridine reductase; dihydropteridine reductase (NADH); 5,6,7,8-tetrahydropteridine:NAD(P)H+ oxidoreductase

Systematic name: 5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase

Comments: The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9074-11-7

References:

1. Harano, T. New diaphorases from Bombyx silkworm eggs. NADH/NADPH cytochrome c reductase activity mediated with 6,7-dimethyltetrahydropterin. Insect Biochem. 2 (1972) 385-399.

2. Hasegawa, H. Dihydropteridine reductase from bovine liver. Purification, crystallization, and isolation of a binary complex with NADH. J. Biochem. (Tokyo) 81 (1977) 169-177. [PMID: 191436]

3. Kaufman, S. Phenylalanine hydroxylase. Methods Enzymol. 5 (1962) 809-816.

4. Lind, K.E. Dihydropteridine reductase. Investigation of the specificity for quinoid dihydropteridine and the inhibition by 2,4-diaminopteridines. Eur. J. Biochem. 25 (1972) 560-562. [PMID: 4402916]

5. Nakanishi, N., Hasegawa, H. and Watabe, S. A new enzyme, NADPH-dihydropteridine reductase in bovine liver. J. Biochem. (Tokyo) 81 (1977) 681-685. [PMID: 16875]

[EC 1.5.1.34 created 1972 as EC 1.6.99.7, modified 1981 (EC 1.6.99.10 created 1978, incorporated 1981), transferred 2003 to EC 1.5.1.34]

[EC 1.5.1.35 Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible. (EC 1.5.1.35 created 2006, deleted 2007)]

EC 1.5.1.36

Accepted name: flavin reductase (NADH)

Reaction: reduced flavin + NAD+ = flavin + NADH + H+

Other name(s): NADH-dependent flavin reductase; flavin:NADH oxidoreductase

Systematic name: flavin:NAD+ oxidoreductase

Comments: The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.

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

References:

1. Galan, B., Diaz, E., Prieto, M.A. and Garcia, J.L. Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182 (2000) 627-636. [PMID: 10633095]

[EC 1.5.1.36 created 2011]

EC 1.5.1.37

Accepted name: FAD reductase (NADH)

Reaction: FADH2 + NAD+ = FAD + NADH + H+

For diagram of reaction click here.

Other name(s): NADH-FAD reductase; NADH-dependent FAD reductase; NADH:FAD oxidoreductase; NADH:flavin adenine dinucleotide oxidoreductase

Systematic name: FADH2:NAD+ oxidoreductase

Comments: The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.

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

References:

1. Gisi, M.R. and Xun, L. Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100. J. Bacteriol. 185 (2003) 2786-2792. [PMID: 12700257]

[EC 1.5.1.37 created 2011]

EC 1.5.1.38

Accepted name: FMN reductase (NADPH)

Reaction: FMNH2 + NADP+ = FMN + NADPH + H+

For diagram of reaction click here.

Other name(s): FRP; flavin reductase P; SsuE

Systematic name: FMNH2:NADP+ oxidoreductase

Comments: The enzymes from bioluminescent bacteria contain FMN [4], while the enzyme from Escherichia coli does not [8]. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].

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

References:

1. Gerlo, E. and Charlier, J. Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi. Eur. J. Biochem. 57 (1975) 461-467. [PMID: 1175652]

2. Jablonski, E. and DeLuca, M. Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry 16 (1977) 2932-2936. [PMID: 880288]

3. Jablonski, E. and DeLuca, M. Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry 17 (1978) 672-678. [PMID: 23827]

4. Lei, B., Liu, M., Huang, S. and Tu, S.C. Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme. J. Bacteriol. 176 (1994) 3552-3558. [PMID: 8206832]

5. Tanner, J.J., Lei, B., Tu, S.C. and Krause, K.L. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry 35 (1996) 13531-13539. [PMID: 8885832]

6. Liu, M., Lei, B., Ding, Q., Lee, J.C. and Tu, S.C. Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium. Arch. Biochem. Biophys. 337 (1997) 89-95. [PMID: 8990272]

7. Lei, B. and Tu, S.C. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623-14629. [PMID: 9772191]

8. Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646. [PMID: 10480865]

[EC 1.5.1.38 created 2011]

EC 1.5.1.39

Accepted name: FMN reductase [NAD(P)H]

Reaction: FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): FRG

Systematic name: FMNH2:NAD(P)+ oxidoreductase

Comments: Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from , FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes [1]. Also reduces riboflavin and FAD, but more slowly.

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

References:

1. Watanabe, H. and Hastings, J.W. Specificities and properties of three reduced pyridine nucleotide-flavin mononucleotide reductases coupling to bacterial luciferase. Mol. Cell. Biochem. 44 (1982) 181-187. [PMID: 6981058]

[EC 1.5.1.39 created 2011]

EC 1.5.1.40

Accepted name: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

Reaction: reduced coenzyme F420 + NADP+ = oxidized coenzyme F420 + NADPH + H+

For diagram of reaction click here.

Other name(s): 8-OH-5dFl:NADPH oxidoreductase

Systematic name: reduced coenzyme F420:NADP+ oxidoreductase

Comments: The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate [1].

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

References:

1. Eker, A.P., Hessels, J.K. and Meerwaldt, R. Characterization of an 8-hydroxy-5-deazaflavin:NADPH oxidoreductase from Streptomyces griseus. Biochim. Biophys. Acta 990 (1989) 80-86. [PMID: 2492438]

[EC 1.5.1.40 created 2011]

EC 1.5.1.41

Accepted name: riboflavin reductase [NAD(P)H]

Reaction: reduced riboflavin + NAD(P)+ = riboflavin + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): NAD(P)H-FMN reductase (ambiguous); NAD(P)H-dependent FMN reductase (ambiguous); NAD(P)H:FMN oxidoreductase (ambiguous); NAD(P)H:flavin oxidoreductase (ambiguous); NAD(P)H2 dehydrogenase (FMN) (ambiguous); NAD(P)H2:FMN oxidoreductase (ambiguous); riboflavin mononucleotide reductase (ambiguous); flavine mononucleotide reductase (ambiguous); riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase; flavin mononucleotide reductase (ambiguous); riboflavine mononucleotide reductase (ambiguous); Fre

Systematic name: riboflavin:NAD(P)+ oxidoreductase

Comments: Catalyses the reduction of soluble flavins by reduced pyridine nucleotides. Highest activity with riboflavin. When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin. When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD [1].

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

References:

1. Fontecave, M., Eliasson, R. and Reichard, P. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 262 (1987) 12325-12331. [PMID: 3305505]

2. Spyrou, G., Haggård-Ljungquist, E., Krook, M., Jörnvall, H., Nilsson, E. and Reichard, P. Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol. 173 (1991) 3673-3679. [PMID: 2050627]

3. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]

[EC 1.5.1.41 created 2011]

EC 1.5.1.42

Accepted name: FMN reductase (NADH)

Reaction: FMNH2 + NAD+ = FMN + NADH + H+

For diagram of reaction click here.

Other name(s): NADH-FMN reductase; NADH-dependent FMN reductase; NADH:FMN oxidoreductase; NADH:flavin oxidoreductase

Systematic name: FMNH2:NAD+ oxidoreductase

Comments: The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2]. While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].

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

References:

1. Fontecave, M., Eliasson, R. and Reichard, P. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase. J. Biol. Chem. 262 (1987) 12325-12331. [PMID: 3305505]

2. Spyrou, G., Haggård-Ljungquist, E., Krook, M., Jörnvall, H., Nilsson, E. and Reichard, P. Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme. J. Bacteriol. 173 (1991) 3673-3679. [PMID: 2050627]

3. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]

[EC 1.5.1.42 created 2011]

EC 1.5.1.43

Accepted name: carboxynorspermidine synthase

Reaction: (1) carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+
(2) carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+

Other name(s): carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name)

Systematic name: carboxynorspermidine:NADP+ oxidoreductase

Comments: The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3].

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

References:

1. Nakao, H., Shinoda, S. and Yamamoto, S. Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus. J. Gen. Microbiol. 137 (1991) 1737-1742. [PMID: 1955861]

2. Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899-9907. [PMID: 19196710]

3. Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota. J. Biol. Chem. 286 (2011) 43301-43312. [PMID: 22025614]

[EC 1.5.1.43 created 2012]

EC 1.5.1.44

Accepted name: festuclavine dehydrogenase

Reaction: festuclavine + NAD+ = 6,8-dimethyl-6,7-didehydroergoline + NADH + H+

For diagram of reaction click here.

Glossary: festuclavine = 6,8β-dimethylergoline

Other name(s): FgaFS; festuclavine synthase

Systematic name: festuclavine:NAD+ oxidoreductase

Comments: The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The reaction proceeds in vivo in the opposite direction to the one shown here.

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

References:

1. Wallwey, C., Matuschek, M., Xie, X.L. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: Conversion of chanoclavine-I aldehyde to festuclavine by the festuclavine synthase FgaFS in the presence of the old yellow enzyme FgaOx3. Org. Biomol. Chem. 8 (2010) 3500-3508. [PMID: 20526482]

[EC 1.5.1.44 created 2012]

EC 1.5.1.45

Accepted name: FAD reductase [NAD(P)H]

Reaction: FADH2 + NAD(P)+ = FAD + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): GTNG_3158 (gene name)

Systematic name: FADH2:NAD(P)+ oxidoreductase

Comments: This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and EC 1.14.14.8, anthranilate 3-monooxygenase (FAD). It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. The enzyme has a slight preference for NADPH as acceptor. cf. EC 1.5.1.37, FAD reductase (NADH).

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

References:

1. Liu, X., Dong, Y., Li, X., Ren, Y., Li, Y., Wang, W., Wang, L. and Feng, L. Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2. Microbiology 156 (2010) 589-595. [PMID: 19942660]

[EC 1.5.1.45 created 2012]

EC 1.5.1.46

Accepted name: agroclavine dehydrogenase

Reaction: agroclavine + NADP+ = 6,8-dimethyl-6,7,8,9-tetradehydroergoline + NADPH + H+

For diagram of reaction click here.

Glossary: agroclavine = 6,8-dimethyl-8,9-didehydroergoline

Other name(s): easG (gene name)

Systematic name: agroclavine:NADP+ oxidoreductase

Comments: The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.

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

References:

1. Matuschek, M., Wallwey, C., Xie, X. and Li, S.M. New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine. Org. Biomol. Chem. 9 (2011) 4328-4335. [PMID: 21494745]

[EC 1.5.1.46 created 2013]

EC 1.5.1.47

Accepted name: dihydromethanopterin reductase [NAD(P)+]

Reaction: 5,6,7,8-tetrahydromethanopterin + NAD(P)+ = 7,8-dihydromethanopterin + NAD(P)H + H+

For diagram of reaction click here.

Other name(s): DmrA; H2MPT reductase; 5,6,7,8-tetrahydromethanopterin 5,6-oxidoreductase; dihydromethanopterin reductase

Systematic name: 5,6,7,8-tetrahydromethanopterin:NAD(P)+ 5,6-oxidoreductase

Comments: The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration [1]. It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).

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

References:

1. Caccamo, M.A., Malone, C.S. and Rasche, M.E. Biochemical characterization of a dihydromethanopterin reductase involved in tetrahydromethanopterin biosynthesis in Methylobacterium extorquens AM1. J. Bacteriol. 186 (2004) 2068-2073. [PMID: 15028691]

[EC 1.5.1.47 created 2013, modified 2014]

EC 1.5.1.48

Accepted name: 2-methyl-1-pyrroline reductase

Reaction: (R)-2-methylpyrrolidine + NADP+ = 2-methyl-1-pyrroline + NADPH + H+

Other name(s): (R)-imine reductase (ambiguous)

Systematic name: (R)-2-methylpyrrolidine:NADP+ 2-oxidoreductase

Comments: The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.

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

References:

1. Mitsukura, K., Suzuki, M., Shinoda, S., Kuramoto, T., Yoshida, T. and Nagasawa, T. Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587. Biosci. Biotechnol. Biochem. 75 (2011) 1778-1782. [PMID: 21897027]

[EC 1.5.1.48 created 2014]

EC 1.5.1.49

Accepted name: 1-pyrroline-2-carboxylate reductase [NAD(P)H]

Reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+

Systematic name: L-proline:NAD(P)+ 2-oxidoreductase

Comments: The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter. While the enzyme is active with both NADH and NADPH, activity is higher with NADPH.

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

References:

1. Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240-250. [PMID: 24649405]

[EC 1.5.1.49 created 2015]

EC 1.5.1.50

Accepted name: dihydromonapterin reductase

Reaction: 5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+

Glossary: 7,8-dihydromonapterin = 2-amino-6-[(1S,2S)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one

Other name(s): FolM; H2-MPt reductase

Systematic name: 5,6,7,8-tetrahydromonapterin:NADP+ oxidoreductase

Comments: The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.

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

References:

1. Pribat, A., Blaby, I.K., Lara-Nunez, A., Gregory, J.F., 3rd, de Crecy-Lagard, V. and Hanson, A.D. FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 192 (2010) 475-482. [PMID: 19897652]

[EC 1.5.1.50 created 2015]

EC 1.5.1.51

Accepted name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase

Reaction: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+

Other name(s): SbnB

Systematic name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)

Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.

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

References:

1. Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11 (2011) 199. [PMID: 21906287]

2. Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379-388. [PMID: 24485762]

[EC 1.5.1.51 created 2017]


EC 1.5.3 With oxygen as acceptor

Contents

EC 1.5.3.1 sarcosine oxidase
EC 1.5.3.2 N-methyl-L-amino-acid oxidase
EC 1.5.3.3 deleted
EC 1.5.3.4 N6-methyl-lysine oxidase
EC 1.5.3.5 (S)-6-hydroxynicotine oxidase
EC 1.5.3.6 (R)-6-hydroxynicotine oxidase
EC 1.5.3.7 L-pipecolate oxidase
EC 1.5.3.8 deleted, included in EC 1.3.3.8
EC 1.5.3.9 now EC 1.21.3.3
EC 1.5.3.10 dimethylglycine oxidase
EC 1.5.3.11 deleted, now EC 1.5.3.13, EC 1.5.3.14, EC 1.5.3.15, EC 1.5.3.16 and EC 1.5.3.17
EC 1.5.3.12 dihydrobenzophenanthridine oxidase

EC 1.5.3.13 N1-acetylpolyamine oxidase
EC 1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)
EC 1.5.3.15 N8-acetylspermidine oxidase (propane-1,3-diamine-forming)
EC 1.5.3.16 spermine oxidase
EC 1.5.3.17 non-specific polyamine oxidase
EC 1.5.3.18 L-saccharopine oxidase
EC 1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)
EC 1.5.3.20 N-alkylglycine oxidase
EC 1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)
EC 1.5.3.22 coenzyme F420H2 oxidase
EC 1.5.3.23 glyphosate oxidoreductase


EC 1.5.3.1

Accepted name: sarcosine oxidase

Reaction: sarcosine + H2O + O2 = glycine + formaldehyde + H2O2

Systematic name: sarcosine:oxygen oxidoreductase (demethylating)

Comments: A flavoprotein (FAD). The flavin is both covalently and non-covalently bound in a molar ratio of 1:1.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-22-5

References:

1. Hayashi, S., Nakamura, S. and Suzuki, M. Corynebacterium sarcosine oxidase: a unique enzyme having covalently-bound and noncovalently-bound flavins. Biochem. Biophys. Res. Commun. 96 (1980) 924-930. [PMID: 6158947]

2. Mori, N., Sano, M., Tani, Y. and Yamada, H. Purification and propertie of sarcosine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1391-1397.

3. Suzuki, M. Purification and some properties of sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. (Tokyo) 89 (1981) 599-607. [PMID: 7240129]

[EC 1.5.3.1 created 1961]

EC 1.5.3.2

Accepted name: N-methyl-L-amino-acid oxidase

Reaction: an N-methyl-L-amino acid + H2O + O2 = an L-amino acid + formaldehyde + H2O2

Other name(s): N-methylamino acid oxidase; demethylase

Systematic name: N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating)

Comments: A flavoprotein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-23-6

References:

1. Moritani, M. Demethylase. IV. Kinetics and reaction mechanism. Hukuoka Acta Med. 43 (1952) 651-658.

2. Moritani, M. Demethylase. V. Specificity and its relation to amino acid oxidase. Hukuoka Acta Med. 43 (1952) 731-735.

3. Moritani, M., Tung, T.-C., Fujii, S., Mito, H., Izumika, N., Kenmochi, K. and Hirohata, R. Specificity of rabbit kidney demethylase. J. Biol. Chem. 209 (1954) 485-492.

[EC 1.5.3.2 created 1961]

[EC 1.5.3.3 Deleted entry: spermine oxidase (EC 1.5.3.3 created 1961, deleted 1972)]

EC 1.5.3.4

Accepted name: N6-methyl-lysine oxidase

Reaction: N6-methyl-L-lysine + H2O + O2 = L-lysine + formaldehyde + H2O2

Other name(s): ε-alkyl-L-lysine:oxygen oxidoreductase ; N6-methyllysine oxidase; ε-N-methyllysine demethylase; ε-alkyllysinase

Systematic name: N6-methyl-L-lysine:oxygen oxidoreductase (demethylating)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-28-3

References:

1. Kim, S., Benoiton, L. and Paik, W.K. α-Alkyllysinase. Purification and properties of the enzyme. J. Biol. Chem. 239 (1964) 3790-3796.

[EC 1.5.3.4 created 1972]

EC 1.5.3.5

Accepted name: (S)-6-hydroxynicotine oxidase

Reaction: (S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction)
(1a) (S)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous)

For diagram of reaction click here.

Glossary: (S)-6-hydroxynicotine = 5-[(2S)-1-methylpyrrolidin-2-yl]pyridin-2-ol
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine

Other name(s): L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name)

Systematic name: (S)-6-hydroxynicotine:oxygen oxidoreductase

Comments: A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6, (R)-6-hydroxynicotine oxidase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37256-29-4

References:

1. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]

2. Dai, V.D., Decker, K. and Sund, H. Purification and properties of L-6-hydroxynicotine oxidase. Eur. J. Biochem. 4 (1968) 95-102. [PMID: 5646150]

3. Schenk, S., Hoelz, A., Krauss, B. and Decker, K. Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol. 284 (1998) 1323-1339. [PMID: 9878353]

4. Qiu, J., Wei, Y., Ma, Y., Wen, R., Wen, Y. and Liu, W. A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7. Appl. Environ. Microbiol. 80 (2014) 5552-5560. [PMID: 25002425]

[EC 1.5.3.5 created 1972, modified 2015]

EC 1.5.3.6

Accepted name: (R)-6-hydroxynicotine oxidase

Reaction: (R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction)
(1a) (R)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2
(1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous)

For diagram of reaction click here.

Glossary: (R)-6-hydroxynicotine = 5-[(2R)-1-methylpyrrolidin-2-yl]pyridin-2-ol
5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine

Other name(s): D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase

Systematic name: (R)-6-hydroxynicotine:oxygen oxidoreductase

Comments: A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the (S)-isomer (cf. EC 1.5.3.5, (S)-6-hydroxynicotine oxidase).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 37233-46-8

References:

1. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]

2. Brühmüller, M., Möhler, H.K. and Decker, K. Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase. Eur. J. Biochem. 29 (1972) 143-151. [PMID: 4628374]

3. Brandsch, R., Hinkkanen, A.E., Mauch, L., Nagursky, H. and Decker, K. 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur. J. Biochem. 167 (1987) 315-320. [PMID: 3622516]

4. Schenk, S., Hoelz, A., Krauss, B. and Decker, K. Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol. 284 (1998) 1323-1339. [PMID: 9878353]

5. Koetter, J.W. and Schulz, G.E. Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans. J. Mol. Biol. 352 (2005) 418-428. [PMID: 16095622]

[EC 1.5.3.6 created 1972, modified 2015]

EC 1.5.3.7

Accepted name: L-pipecolate oxidase

Reaction: L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2

Glossary: L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

Other name(s): pipecolate oxidase; L-pipecolic acid oxidase

Systematic name: L-pipecolate:oxygen 1,6-oxidoreductase

Comments: The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 81669-65-0

References:

1. Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034-1039. [PMID: 6051341]

2. Kinzel, J.J. and Bhattacharjee, J.K. Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase. J. Bacteriol. 151 (1982) 1073-1077. [PMID: 6809728]

[EC 1.5.3.7 created 1986]

[EC 1.5.3.8 Deleted entry: now included with EC 1.3.3.8 tetrahydroberberine oxidase (EC 1.5.3.8 created 1989, deleted 1992)]

[EC 1.5.3.9 Transferred entry: now EC 1.21.3.3, reticuline oxidase (EC 1.5.3.9 created 1989, modified 1999, deleted 2002)]

EC 1.5.3.10

Accepted name: dimethylglycine oxidase

Reaction: N,N-dimethylglycine + H2O + O2 = sarcosine + formaldehyde + H2O2

Systematic name: N,N-dimethylglycine:oxygen oxidoreductase (demethylating)

Comments: A flavoprotein (FAD). Does not oxidize sarcosine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-30-7

References:

1. Mori, N., Kawakami, B., Tani, Y. and Yamada, H. Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1383-1389.

[EC 1.5.3.10 created 1992]

[EC 1.5.3.11 Deleted entry: Now included with EC 1.5.3.13 N1-acetylpolyamine oxidase, EC 1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming), EC 1.5.3.15 N8-acetylspermidine oxidase (propane-1,3-diamine-forming), EC 1.5.3.16 spermine oxidase and EC 1.5.3.17 non-specific polyamine oxidase (EC 1.5.3.11 created 1992, deleted 2009)]

EC 1.5.3.12

Accepted name: dihydrobenzophenanthridine oxidase

Reaction: (1) dihydrosanguinarine + O2 = sanguinarine + H2O2;

(2) dihydrochelirubine + O2 = chelirubine + H2O2;

(3) dihydromacarpine + O2 = macarpine + H2O2

For diagram click here.

Systematic name: dihydrobenzophenanthridine:oxygen oxidoreductase

Comments: a CuII enzyme found in higher plants that produces oxidized forms of the benzophenanthridine alkaloids

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 114051-83-1

References:

1. Schumacher, H.-M. and Zenk, M.H. Partial purification and characterization of dihydrobenzophenanthridine oxidase from Eschscholtzia tenuifolia cell suspension cultures. Plant Cell Reports 7 (1988) 43-46.

2. Arakawa, H., Clark, W.G., Psenak. M. and Coscia, C.J. Purification and characterization of dihydrobenzophenanthridine oxidase from elicited Sanguinaria canadensis cell cultures. Arch. Biochem. Biophys. 299 (1992) 1-7. [PMID: 1444440]

[EC 1.5.3.12 created 1999]

EC 1.5.3.13

Accepted name: N1-acetylpolyamine oxidase

Reaction: (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
(2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2

Other name(s): hPAO-1; PAO (ambiguous); mPAO; hPAO; polyamine oxidase (ambiguous)

Systematic name: N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)

Comments: The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).

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

References:

1. Vujcic, S., Liang, P., Diegelman, P., Kramer, D.L. and Porter, C.W. Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem. J. 370 (2003) 19-28. [PMID: 12477380]

2. Jarvinen, A., Grigorenko, N., Khomutov, A.R., Hyvonen, M.T., Uimari, A., Vepsalainen, J., Sinervirta, R., Keinanen, T.A., Vujcic, S., Alhonen, L., Porter, C.W. and Janne, J. Metabolic stability of α-methylated polyamine derivatives and their use as substitutes for the natural polyamines. J. Biol. Chem. 280 (2005) 6595-6601. [PMID: 15611107]

3. Wang, Y., Hacker, A., Murray-Stewart, T., Frydman, B., Valasinas, A., Fraser, A.V., Woster, P.M. and Casero, R.A., Jr. Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity. Cancer Chemother Pharmacol 56 (2005) 83-90. [PMID: 15791459]

4. Wu, T., Yankovskaya, V. and McIntire, W.S. Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J. Biol. Chem. 278 (2003) 20514-20525. [PMID: 12660232]

[EC 1.5.3.13 created 2009]

EC 1.5.3.14

Accepted name: polyamine oxidase (propane-1,3-diamine-forming)

Reaction: spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2

Other name(s): MPAO; maize PAO

Systematic name: spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)

Comments: As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).

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

References:

1. Tavladoraki, P., Schinina, M.E., Cecconi, F., Di Agostino, S., Manera, F., Rea, G., Mariottini, P., Federico, R. and Angelini, R. Maize polyamine oxidase: primary structure from protein and cDNA sequencing. FEBS Lett. 426 (1998) 62-66. [PMID: 9598979]

2. Federico, R., Ercolini, L., Laurenzi, M., Angelini, R. Oxidation of acetylpolyamines by maize polyamine oxidase. Phytochemistry 43 (1996) 339-341.

[EC 1.5.3.14 created 2009]

EC 1.5.3.15

Accepted name: N8-acetylspermidine oxidase (propane-1,3-diamine-forming)

Reaction: N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2

Systematic name: N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming)

Comments: Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).

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

References:

1. Shukla, O.P., Muller, S. and Walter, R.D. Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine. Mol. Biochem. Parasitol. 51 (1992) 91-98. [PMID: 1565141]

[EC 1.5.3.15 created 2009]

EC 1.5.3.16

Accepted name: spermine oxidase

Reaction: spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2

Other name(s): PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu

Systematic name: spermidine:oxygen oxidoreductase (spermidine-forming)

Comments: The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)] and EC 1.5.3.17 (non-specific polyamine oxidase).

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

References:

1. Murray-Stewart, T., Wang, Y., Goodwin, A., Hacker, A., Meeker, A. and Casero, R.A., Jr. Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology. FEBS J. 275 (2008) 2795-2806. [PMID: 18422650]

2. Cervelli, M., Polticelli, F., Federico, R. and Mariottini, P. Heterologous expression and characterization of mouse spermine oxidase. J. Biol. Chem. 278 (2003) 5271-5276. [PMID: 12458219]

3. Tavladoraki, P., Rossi, M.N., Saccuti, G., Perez-Amador, M.A., Polticelli, F., Angelini, R. and Federico, R. Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion. Plant Physiol. 141 (2006) 1519-1532. [PMID: 16778015]

4. Wang, Y., Murray-Stewart, T., Devereux, W., Hacker, A., Frydman, B., Woster, P.M. and Casero, R.A., Jr. Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem. Biophys. Res. Commun. 304 (2003) 605-611. [PMID: 12727196]

[EC 1.5.3.16 created 2009]

EC 1.5.3.17

Accepted name: non-specific polyamine oxidase

Reaction: (1) spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
(2) spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2
(3) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
(4) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2

Other name(s): polyamine oxidase (ambiguous); Fms1; AtPAO3

Systematic name: polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)

Comments: A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)] and EC 1.5.3.16 (spermine oxidase).

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

References:

1. Moschou, P.N., Sanmartin, M., Andriopoulou, A.H., Rojo, E., Sanchez-Serrano, J.J. and Roubelakis-Angelakis, K.A. Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis. Plant Physiol. 147 (2008) 1845-1857. [PMID: 18583528]

2. Muller, S. and Walter, R.D. Purification and characterization of polyamine oxidase from Ascaris suum. Biochem. J. 283 (1992) 75-80. [PMID: 1567380]

3. Landry, J. and Sternglanz, R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem. Biophys. Res. Commun. 303 (2003) 771-776. [PMID: 12670477]

[EC 1.5.3.17 created 2009]

EC 1.5.3.18

Accepted name: L-saccharopine oxidase

Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 = (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2

Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine

Other name(s): FAP2

Systematic name: L-saccharopine:oxygen oxidoreductase (L-glutamate forming)

Comments: The enzyme is involved in pipecolic acid biosynthesis. A flavoprotein (FAD).

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

References:

1. Yoshida, N., Akazawa, S., Katsuragi, T. and Tani, Y. Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe. J. Biosci. Bioeng. 97 (2004) 278-280. [PMID: 16233628]

2. Wickwire, B.M., Wagner, C. and Broquist, H.P. Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis. J. Biol. Chem. 265 (1990) 14748-14753. [PMID: 2394693]

[EC 1.5.3.18 created 2011]

EC 1.5.3.19

Accepted name: 4-methylaminobutanoate oxidase (formaldehyde-forming)

Reaction: 4-methylaminobutanoate + O2 + H2O = 4-aminobutanoate + formaldehyde + H2O2

For diagram of reaction click here.

Other name(s): mabO (gene name)

Systematic name: 4-methylaminobutanoate:oxygen oxidoreductase (formaldehyde-forming)

Comments: A flavoprotein (FAD). In the enzyme from the soil bacterium Arthrobacter nicotinovorans the cofactor is covalently bound. Participates in the nicotine degradation pathway of this organism.

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

References:

1. Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677-4684. [PMID: 15606755]

[EC 1.5.3.19 created 2012]

EC 1.5.3.20

Accepted name: N-alkylglycine oxidase

Reaction: N-alkylglycine + H2O + O2 = alkylamine + glyoxalate + H2O2

Other name(s): N-carboxymethylalkylamine:oxygen oxidoreductase (decarboxymethylating)

Systematic name: N-alkylglycine:oxygen oxidoreductase (alkylamine forming)

Comments: Isolated from the mold Cladosporium sp. G-10. Acts on N6-(carboxymethyl)lysine, 6-[(carboxymethy)amino]hexanoic acid, sarcosine and N-ethylglycine. It has negligible action on glycine (cf. EC 1.4.3.19 glycine oxidase).

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

References:

1. Gomi, K. and Horiuchi, T. Purification and characterization of a new enzyme, N-alkylglycine oxidase from Cladosporium sp. G-10. Biochim. Biophys. Acta 1429 (1999) 439-445. [PMID: 9989229]

[EC 1.5.3.20 created 2012]

EC 1.5.3.21

Accepted name: 4-methylaminobutanoate oxidase (methylamine-forming)

Reaction: 4-methylaminobutanoate + O2 + H2O = succinate semialdehyde + methylamine + H2O2

For diagram of reaction click here.

Other name(s): mao (gene name, ambiguous)

Systematic name: 4-methylaminobutanoate methylamidohydrolase

Comments: The enzyme participates in the nicotine degradation pathway of the soil bacterium Arthrobacter nicotinovorans. Has a very weak monoamine oxidase (EC 1.4.3.4) activity with 4-aminobutanoate [1].

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

References:

1. Chiribau, C.B., Sandu, C., Fraaije, M., Schiltz, E. and Brandsch, R. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271 (2004) 4677-4684. [PMID: 15606755]

2. Chiribau, C.B., Mihasan, M., Ganas, P., Igloi, G.L., Artenie, V. and Brandsch, R. Final steps in the catabolism of nicotine. FEBS J. 273 (2006) 1528-1536. [PMID: 16689938]

[EC 1.5.3.21 created 2012]

EC 1.5.3.22

Accepted name: coenzyme F420H2 oxidase

Reaction: 2 reduced coenzyme F420 + O2 = 2 oxidized coenzyme F420 + 2 H2O

Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate

Other name(s): FprA

Systematic name: reduced coenzyme F420:oxygen oxidoreductase

Comments: The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C-5 of coenzyme F420 [2].

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

References:

1. Seedorf, H., Dreisbach, A., Hedderich, R., Shima, S. and Thauer, R.K. F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification. Arch. Microbiol. 182 (2004) 126-137. [PMID: 15340796]

2. Seedorf, H., Kahnt, J., Pierik, A.J. and Thauer, R.K. Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from methanogenic Archaea as determined by mass spectrometry. FEBS J. 272 (2005) 5337-5342. [PMID: 16218963]

3. Seedorf, H., Hagemeier, C.H., Shima, S., Thauer, R.K., Warkentin, E. and Ermler, U. Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O. FEBS J. 274 (2007) 1588-1599. [PMID: 17480207]

[EC 1.5.3.22 created 2013]

EC 1.5.3.23

Accepted name: glyphosate oxidoreductase

Reaction: 2 glyphosate + O2 = 2 aminomethylphosphonate + 2 glyoxylate

Glossary: glyphosate = N-(phosphonomethyl)glycine

Other name(s): gox (gene name)

Systematic name: glyphosate oxidoreductase (aminomethylphosphonate-forming)

Comments: The enzyme, characterized from the bacterium Ochrobactrum sp. G-1, contains an FAD cofactor. The catalytic cycle starts with a reduction of the FAD cofactor by one molecule of glyphosate, yielding reduced FAD and a Schiff base of aminomethylphosphonate with glyoxylate that is hydrolysed to the single components. The reduced FAD is reoxidized by oxygen, generating water and an oxygenated flavin intermediate, which catalyses the oxygenation of a second molecule of glyphosate, forming the second pair of aminomethylphosphonate and glyoxylate.

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

References:

1. Barry, G. F. and Kishore. G. M. Glyphosate tolerant plants. US patent US5463175, (1995).

2. Sviridov, A.V., Shushkova, T.V., Zelenkova, N.F., Vinokurova, N.G., Morgunov, I.G., Ermakova, I.T. and Leontievsky, A.A. Distribution of glyphosate and methylphosphonate catabolism systems in soil bacteria Ochrobactrum anthropi and Achromobacter sp. Appl. Microbiol. Biotechnol. 93 (2012) 787-796. [PMID: 21789492]

[EC 1.5.3.23 created 2016]


EC 1.5.4 With disulfide as acceptor

EC 1.5.4.1

Accepted name: pyrimidodiazepine synthase

Reaction: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one + glutathione disulfide + H2O = 6-pyruvoyltetrahydropterin + 2 glutathione

For diagram of reaction click here.

Glossary: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one = pyrimidodiazepine

Other name(s): PDA synthase; pyrimidodiazepine:oxidized-glutathione oxidoreductase (ring-opening, cyclizing); pyrimidodiazepine:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)

Systematic name: 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-b][1,4]diazepin-4-one:glutathione-disulfide oxidoreductase (ring-opening, cyclizing)

Comments: In the reverse direction, the reduction of 6-pyruvoyl-tetrahydropterin is accompanied by the opening of the 6-membered pyrazine ring and the formation of the 7-membered diazepine ring. The pyrimidodiazepine formed is an acetyldihydro derivative. Involved in the formation of the eye pigment drosopterin in Drosophila melanogaster.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93586-06-2

References:

1. Wiederrecht, G.J. and Brown, G.M. Purification and properties of the enzymes from Drosophila melanogaster that catalyze the conversion of dihydroneopterin triphosphate to the pyrimidodiazepine precursor of the drosopterins. J. Biol. Chem. 259 (1984) 14121-14127. [PMID: 6438092]

2. Kim, J., Suh, H., Kim, S., Kim, K., Ahn, C. and Yim, J. Identification and characteristics of the structural gene for the Drosophila eye colour mutant sepia, encoding PDA synthase, a member of the ω class glutathione S-transferases. Biochem. J. 398 (2006) 451-460. [PMID: 16712527]

[EC 1.5.4.1 created 1990, modified 2014]


EC 1.5.5 With a quinone or similar compound as acceptor

Contents

EC 1.5.5.1 electron-transferring-flavoprotein dehydrogenase
EC 1.5.5.2 proline dehydrogenase
EC 1.5.5.3 hydroxyproline dehydrogenase

EC 1.5.5.1

Accepted name: electron-transferring-flavoprotein dehydrogenase

Reaction: reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol

Other name(s): ETF-QO; ETF:ubiquinone oxidoreductase; electron transfer flavoprotein dehydrogenase; electron transfer flavoprotein Q oxidoreductase; electron transfer flavoprotein-ubiquinone oxidoreductase; electron transfer flavoprotein reductase

Systematic name: electron-transferring-flavoprotein:ubiquinone oxidoreductase

Comments: An iron-sulfur flavoprotein, forming part of the mitochondrial electron-transfer system.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 86551-03-3

References:

1. Beckmann, J.D. and Frerman, F.E. Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties. Biochemistry 24 (1985) 3913-3921. [PMID: 4052375]

2. Ruzicka, F.J. and Beinhert, H. A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid β-oxidation pathway. J. Biol. Chem. 252 (1977) 8440-8445. [PMID: 925004]

[EC 1.5.5.1 created 1986]

EC 1.5.5.2

Accepted name: proline dehydrogenase

Reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol

Other name(s): L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase

Systematic name: L-proline:quinone oxidoreductase

Comments: A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9050-70-8

References:

1. Scarpulla, R.C. and Sofer, R.L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J. Biol. Chem. 253 (1978) 5997-6001. [PMID: 355248]

2. Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086-13092. [PMID: 1618807]

3. Moxley, M.A., Tanner, J.J. and Becker, D.F. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516 (2011) 113-120. [PMID: 22040654]

[EC 1.5.5.2 created 1980 as 1.5.99.8, transferred 2013 to 1.5.5.2]

EC 1.5.5.3

Accepted name: hydroxyproline dehydrogenase

Reaction: trans-4-hydroxy-L-proline + a quinone = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol

Other name(s): HYPDH; OH-POX; hydroxyproline oxidase; PRODH2 (gene name)

Systematic name: trans-4-hydroxy-L-proline:quinone oxidoreductase

Comments: A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).

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

References:

1. Cooper, S.K., Pandhare, J., Donald, S.P. and Phang, J.M. A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species. J. Biol. Chem. 283 (2008) 10485-10492. [PMID: 18287100]

2. Summitt, C.B., Johnson, L.C., Jonsson, T.J., Parsonage, D., Holmes, R.P. and Lowther, W.T. Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. Biochem. J. 466 (2015) 273-281. [PMID: 25697095]

[EC 1.5.5.3 created 2017]


EC 1.5.7 With an iron-sulfur protein as acceptor

Contents

EC 1.5.7.1 methylenetetrahydrofolate reductase (ferredoxin)
EC 1.5.7.2 coenzyme F420 oxidoreductase (ferredoxin)

EC 1.5.7.1

Accepted name: methylenetetrahydrofolate reductase (ferredoxin)

Reaction: 5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+

Other name(s): 5,10-methylenetetrahydrofolate reductase

Systematic name: 5-methyltetrahydrofolate:ferredoxin oxidoreductase

Comments: An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H.

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

References:

1. Clark, J.E. and Ljungdahl, L.G. Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum. J. Biol. Chem. 259 (1984) 10845-10849. [PMID: 6381490]

[EC 1.5.7.1 created 2005]

EC 1.5.7.2

Accepted name: coenzyme F420 oxidoreductase (ferredoxin)

Reaction: reduced coenzyme F420 + 2 oxidized ferredoxin = oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+

For diagram of reaction, click here

Glossary: oxidized coenzyme F420 = N-(N-{O-[5-(8-hydroxy-2,4-dioxo-2,3,4,10-tetrahydropyrimido[4,5-b]quinolin-10-yl)-5-deoxy-L-ribityl-1-phospho]-(S)-lactyl}-γ-L-glutamyl)-L-glutamate

Other name(s): Fd:F420 oxidoreductase; FpoF protein; ferredoxin:F420 oxidoreductase

Systematic name: coenzyme F420:ferredoxin oxidoreductase

Comments: The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.

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

References:

1. Welte, C. and Deppenmeier, U. Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei. FEBS J. 278 (2011) 1277-1287. [PMID: 21306561]

[EC 1.5.7.2 created 2013]


EC 1.5.8 With a flavin as acceptor

Contents

EC 1.5.8.1 dimethylamine dehydrogenase
EC 1.5.8.2 trimethylamine dehydrogenase
EC 1.5.8.3 sarcosine dehydrogenase
EC 1.5.8.4 dimethylglycine dehydrogenase

EC 1.5.8.1

Accepted name: dimethylamine dehydrogenase

Reaction: dimethylamine + H2O + electron-transfer flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein

Systematic name: dimethylamine:electron-transferring flavoprotein oxidoreductase

Comments: Contains FAD and a [4Fe-4S] cluster.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 68247-64-3

References:

1. Yang, C.C., Packman, L.C. and Scrutton, N.S. The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition. Eur. J. Biochem. 232 (1995) 264-271. [PMID: 7556160]

[EC 1.5.8.1 created 1999 as EC 1.5.99.10, transferred 2002 to EC 1.5.8.1]

EC 1.5.8.2

Accepted name: trimethylamine dehydrogenase

Reaction: trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

Systematic name: trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating)

Comments: A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 39307-09-0

References:

1. Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P-10P.

2. Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361-369. [PMID: 204297]

3. Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958-23965. [PMID: 7592591]

4. Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457-8465. [PMID: 11756429]

5. Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145-181. [PMID: 11192721]

[EC 1.5.8.2 created 1976 as EC 1.5.99.7, transferred 2002 to EC 1.5.8.2]

EC 1.5.8.3

Accepted name: sarcosine dehydrogenase

Reaction: sarcosine + H2O + electron-transfer flavoprotein = glycine + formaldehyde + reduced electron-transfer flavoprotein

Other name(s): sarcosine N-demethylase; monomethylglycine dehydrogenase; sarcosine:(acceptor) oxidoreductase (demethylating)

Systematic name: sarcosine:electron-transfer flavoprotein oxidoreductase (demethylating)

Comments: A flavoprotein (FMN). Tetrahydrofolate is also a substrate, being converted to N5,N10-methylenetetrahydrofolate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37228-65-2, 93389-49-2

References:

1. Hoskins, D.D. and MacKenzie, C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236 (1961) 177-183. [PMID: 13716069]

2. Frisell, W.R. and MacKenzie, C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237 (1962) 94-98. [PMID: 13895406]

3. Steenkamp, D.J. and Husain, M. The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem. J. 203 (1982) 707-715. [PMID: 6180732]

[EC 1.5.8.3 created 1972 as EC 1.5.99.1, transferred 2012 to EC 1.5.8.3]

EC 1.5.8.4

Accepted name: dimethylglycine dehydrogenase

Reaction: N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + electron-transfer flavoprotein = sarcosine + 5,10-methylenetetrahydrofolate + reduced electron-transfer flavoprotein

Glossary: sarcosine = N-methylglycine

Other name(s): N,N-dimethylglycine oxidase; N,N-dimethylglycine:(acceptor) oxidoreductase (demethylating); Me2GlyDH; N,N-dimethylglycine:electron-transfer flavoprotein oxidoreductase (demethylating)

Systematic name: N,N-dimethylglycine,5,6,7,8-tetrahydrofolate:electron-transferflavoprotein oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming)

Comments: A flavoprotein, containing a histidyl(Nπ)-(8α)FAD linkage at position 91 in the human protein. An imine intermediate is channeled from the FAD binding site to the 5,6,7,8-tetrahydrofolate binding site through a 40 Å tunnel [5,8,9]. In the absence of 5,6,7,8-tetrahydrofolate the enzyme forms formaldehyde [5,9].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-30-7

References:

1. Frisell, W.R. and MacKenzie, C.G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 237 (1962) 94-98. [PMID: 13895406]

2. Hoskins, D.D. and MacKenzie, C.G. Solubilization and electron transfer flavoprotein requirement of mitochondrial sarcosine dehydrogenase and dimethylglycine dehydrogenase. J. Biol. Chem. 236 (1961) 177-183. [PMID: 13716069]

3. Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics. J. Biol. Chem. 256 (1981) 4102-4108. [PMID: 6163777]

4. Wittwer, A.J. and Wagner, C. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Flavoprotein nature and enzymatic properties of the purified proteins. J. Biol. Chem. 256 (1981) 4109-4115. [PMID: 6163778]

5. Porter, D.H., Cook, R.J. and Wagner, C. Enzymatic properties of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver. Arch. Biochem. Biophys. 243 (1985) 396-407. [PMID: 2417560]

6. Brizio, C., Brandsch, R., Bufano, D., Pochini, L., Indiveri, C. and Barile, M. Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase. Protein Expr. Purif. 37 (2004) 434-442. [PMID: 15358367]

7. Brizio, C., Brandsch, R., Douka, M., Wait, R. and Barile, M. The purified recombinant precursor of rat mitochondrial dimethylglycine dehydrogenase binds FAD via an autocatalytic reaction. Int. J. Biol. Macromol. 42 (2008) 455-462. [PMID: 18423846]

8. Luka, Z., Pakhomova, S., Loukachevitch, L.V., Newcomer, M.E. and Wagner, C. Folate in demethylation: the crystal structure of the rat dimethylglycine dehydrogenase complexed with tetrahydrofolate. Biochem. Biophys. Res. Commun. 449 (2014) 392-398. [PMID: 24858690]

9. Augustin, P., Hromic, A., Pavkov-Keller, T., Gruber, K. and Macheroux, P. Structure and biochemical properties of recombinant human dimethylglycine dehydrogenase and comparison to the disease-related H109R variant. FEBS J. 283 (2016) 3587-3603. [PMID: 27486859]

[EC 1.5.8.4 created 1972 as EC 1.5.99.2, transferred 2012 to EC 1.5.8.4, modified 2017]


EC 1.5.98 With other, known, physiological acceptor

Contents

EC 1.5.98.1 methylenetetrahydromethanopterin dehydrogenase
EC 1.5.98.2 5,10-methylenetetrahydromethanopterin reductase
EC 1.5.98.3 coenzyme F420:methanophenazine dehydrogenase

EC 1.5.98.1

Accepted name: methylenetetrahydromethanopterin dehydrogenase

Reaction: 5,10-methylenetetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420

For diagram of reaction click here.

Other name(s): N5,N10-methylenetetrahydromethanopterin dehydrogenase; 5,10-methylenetetrahydromethanopterin dehydrogenase

Systematic name: 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase

Comments: Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin derivative; methanopterin is a pterin analogue. The enzyme is involved in the formation of methane from CO2 in the methanogen Methanothermobacter thermautotrophicus.

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

References:

1. Hartzell, P.L., Zvilius, G., Escalante-Semerena, J.C. and Donnelly, M.I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 133 (1985) 884-890. [PMID: 4084309]

2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]

[EC 1.5.98.1 created 1989 as EC 1.5.99.9, modified 2004, transferred to EC 1.5.98.1 2013]

EC 1.5.98.2

Accepted name: 5,10-methylenetetrahydromethanopterin reductase

Reaction: 5-methyltetrahydromethanopterin + oxidized coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420

For diagram of reaction click here.

Other name(s): 5,10-methylenetetrahydromethanopterin cyclohydrolase; N5,N10-methylenetetrahydromethanopterin reductase; methylene-H4MPT reductase; coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase; N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase

Systematic name: 5-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase

Comments: Catalyses an intermediate step in methanogenesis from CO2 and H2 in methanogenic archaebacteria.

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

References:

1. Ma, K. and Thauer, R.K. Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 191 (1990) 187-193. [PMID: 2379499]

2. te Brömmelstroet, B.W., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri. Biochim. Biophys. Acta 1079 (1991) 293-302. [PMID: 1911853]

3. Ma, K. and Thauer, R.K. Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B. FEBS Lett. 268 (1990) 59-62. [PMID: 1696553]

4. te Brömmelstroet, B.W., Hensgens, C.M., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain ΔH*. J. Biol. Chem. 265 (1990) 1852-1857. [PMID: 2298726]

5. te Brömmelstroet, B.W., Hensgens, C.M., Geerts, W.J., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri. J. Bacteriol. 172 (1990) 564-571. [PMID: 2298699]

[EC 1.5.98.2 created 2000 as EC 1.5.99.11, modified 2004, transferred to EC 1.5.98.2 2013]

EC 1.5.98.3

Accepted name: coenzyme F420:methanophenazine dehydrogenase

Reaction: reduced coenzyme F420 + methanophenazine = oxidized coenzyme F420 + dihydromethanophenazine

Glossary: methanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}phenazine
dihydromethanophenazine = 2-{[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl]oxy}-5,10-dihydrophenazine

Other name(s): F420H2 dehydrogenase; fpoBCDIF (gene names)

Systematic name: reduced coenzyme F420:methanophenazine oxidoreductase

Comments: The enzyme, found in some methanogenic archaea, is responsible for the reoxidation of coenzyme F420, which is reduced during methanogenesis, and for the reduction of methanophenazine to dihydromethanophenazine, which is required by EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase. The enzyme is membrane-bound, and is coupled to proton translocation across the cytoplasmic membrane, generating a proton motive force that is used for ATP generation.

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

References:

1. Brodersen, J., Gottschalk, G. and Deppenmeier, U. Membrane-bound F420H2-dependent heterodisulfide reduction in Methanococcus volta. Arch. Microbiol. 171 (1999) 115-121. [PMID: 9914308]

2. Baumer, S., Ide, T., Jacobi, C., Johann, A., Gottschalk, G. and Deppenmeier, U. The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases. J. Biol. Chem. 275 (2000) 17968-17973. [PMID: 10751389]

3. Deppenmeier, U. The membrane-bound electron transport system of Methanosarcina species. J. Bioenerg. Biomembr. 36 (2004) 55-64. [PMID: 15168610]

4. Abken H. J. and Deppenmeier, U. Purification and properties of an F420H2 dehydrogenase from Methanosarcina mazei Gö1. FEMS Microbiol. Lett. 154 (2006) 231-237.

[EC 1.5.98.3 created 2017]


EC 1.5.99 With unknown physiological acceptor

Contents

EC 1.5.99.1 transferred now EC 1.5.8.3
EC 1.5.99.2 transferred now EC 1.5.8.4
EC 1.5.99.3 L-pipecolate dehydrogenase
EC 1.5.99.4 nicotine dehydrogenase
EC 1.5.99.5 methylglutamate dehydrogenase
EC 1.5.99.6 spermidine dehydrogenase
EC 1.5.99.7 now EC 1.5.8.2
EC 1.5.99.8 transferred now EC 1.5.5.2
EC 1.5.99.9 transferred now EC 1.5.98.1
EC 1.5.99.10 now EC 1.5.8.1
EC 1.5.99.11 transferred now EC 1.5.98.2
EC 1.5.99.12 cytokinin dehydrogenase

EC 1.5.99.13 D-proline dehydrogenase
EC 1.5.99.14 6-hydroxypseudooxynicotine dehydrogenase
EC 1.5.99.15 dihydromethanopterin reductase (acceptor)


[EC 1.5.99.1 Transferred entry: sarcosine dehydrogenase. Now EC 1.5.8.3, sarcosine dehydrogenase (EC 1.5.99.1 created 1972, deleted 2012)]

[EC 1.5.99.2 Transferred entry: dimethylglycine dehydrogenase. Now EC 1.5.8.4, dimethylglycine dehydrogenase (EC 1.5.99.2 created 1972, deleted 2012)]

EC 1.5.99.3

Accepted name: L-pipecolate dehydrogenase

Reaction: L-pipecolate + acceptor = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor

Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate

Other name(s): L-pipecolate:(acceptor) 1,6-oxidoreductase

Systematic name: L-pipecolate:acceptor 1,6-oxidoreductase

Comments: The product reacts with water to form 2-aminoadipate 6-semialdehyde, i.e. 2-amino-6-oxohexanoate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-63-5

References:

1. Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034-1039. [PMID: 6051341]

[EC 1.5.99.3 created 1972, modified 1986]

EC 1.5.99.4

Accepted name: nicotine dehydrogenase

Reaction: (S)-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor

For diagram of reaction click here.

Other name(s): nicotine oxidase; D-nicotine oxidase; nicotine:(acceptor) 6-oxidoreductase (hydroxylating)

Systematic name: nicotine:acceptor 6-oxidoreductase (hydroxylating)

Comments: A metalloprotein (FMN). The enzyme can act on both the naturally found (S)-enantiomer and the synthetic (R)-enantiomer of nicotine, with retention of configuration in both cases [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 37256-31-8

References:

1. Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923-945. [PMID: 13475371]

2. Decker, K. and Bleeg, H. Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta 105 (1965) 313-324. [PMID: 5849820]

3. Hochstein, L.I. and Dalton, B.P. The purification and properties of nicotine oxidase. Biochim. Biophys. Acta 139 (1967) 56-68. [PMID: 4962139]

4. Hochstein, L.I. and Rittenberg, S.C. The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine. J. Biol. Chem. 234 (1959) 156-160. [PMID: 13610912]

[EC 1.5.99.4 created 1972]

EC 1.5.99.5

Accepted name: methylglutamate dehydrogenase

Reaction: N-methyl-L-glutamate + acceptor + H2O = L-glutamate + formaldehyde + reduced acceptor

Other name(s): N-methylglutamate dehydrogenase; N-methyl-L-glutamate:(acceptor) oxidoreductase (demethylating)

Systematic name: N-methyl-L-glutamate:acceptor oxidoreductase (demethylating)

Comments: A number of N-methyl-substituted amino acids can act as donor; 2,6-dichloroindophenol is the best acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37217-26-8

References:

1. Hersh, L.B., Stark, M.J., Worthen, S. and Fiero, M.K. N-Methylglutamate dehydrogenase: kinetic studies on the solubilized enzyme. Arch. Biochem. Biophys. 150 (1972) 219-226. [PMID: 5028076]

[EC 1.5.99.5 created 1976]

EC 1.5.99.6

Accepted name: spermidine dehydrogenase

Reaction: spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor

Glossary: spermidine

Other name(s): spermidine:(acceptor) oxidoreductase

Systematic name: spermidine:acceptor oxidoreductase

Comments: A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9076-64-6

References:

1. Tabor, C.W. and Kellogg, P.D. Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. Biol. Chem. 245 (1970) 5424-5433.

2. Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225-226.

[EC 1.5.99.6 created 1976]

[EC 1.5.99.7 Transferred entry: now EC 1.5.8.2, trimethylamine dehydrogenase (EC 1.5.99.7 created 1976, deleted 2002)]

[EC 1.5.99.8 Transferred entry: proline dehydrogenase. Now EC 1.5.5.2, proline dehydrogenase. (EC 1.5.99.8 created 1980, transferred 2013 to 1.5.5.2, deleted 2013)]

[EC 1.5.99.9 Transferred entry: methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.1, methylenetetrahydromethanopterin dehydrogenase (EC 1.5.99.9 created 1989, modified 2004, deleted 2013)]

[EC 1.5.99.10 Transferred entry: now EC 1.5.8.1, dimethylamine dehydrogenase (EC 1.5.99.10 created 1999, deleted 2002)]

[EC 1.5.99.11 Transferred entry: methylenetetrahydromethanopterin dehydrogenase. As the acceptor is known the enzyme has been transferred to EC 1.5.98.2,5,10-methylenetetrahydromethanopterin reductase (EC 1.5.99.11 created 2000, modified 2004, deleted 2013)]

EC 1.5.99.12

Accepted name: cytokinin dehydrogenase

Reaction: N6-dimethylallyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor

Glossary: zeatin = (E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol = (E)-N6-(4-hydroxy-3-methylbut-2-enyl)adenine

Other name(s): N6-dimethylallyladenine:(acceptor) oxidoreductase; 6-N-dimethylallyladenine:acceptor oxidoreductase; OsCKX2; CKX; cytokinin oxidase/dehydrogenase

Systematic name: N6-dimethylallyladenine:acceptor oxidoreductase

Comments: A flavoprotein(FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a dimethylallyl or other prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 55326-39-1

References:

1. Galuszka, P., Frebort, I., Sebela, M., Jacobsen, S. and Pec, P. Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in plants. Eur. J. Biochem. 268 (2001) 450-461. [PMID: 11168382]

2. Ashikari, M., Sakakibara, H., Lin, S., Yamamoto, T., Takashi, T., Nishimura, A., Angeles, E.R., Qian, Q., Kitano, H. and Matsuoka, M. Cytokinin oxidase regulates rice grain production. Science 309 (2005) 741-745. [PMID: 15976269]

[EC 1.5.99.12 created 2001]

EC 1.5.99.13

Accepted name: D-proline dehydrogenase

Reaction: D-proline + oxidized acceptor = 1-pyrroline-2-carboxylate + reduced acceptor

Other name(s): D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase

Systematic name: D-proline:acceptor oxidoreductase

Comments: A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.

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

References:

1. Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal Chim Acta 619 (2008) 215-220. [PMID: 18558115]

2. Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861-12867. [PMID: 11823469]

[EC 1.5.99.13 created 2010]

EC 1.5.99.14

Accepted name: 6-hydroxypseudooxynicotine dehydrogenase

Reaction: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor

For diagram of reaction click here.

Glossary: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine

Systematic name: 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)

Comments: Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].

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

References:

1. Freudenberg, W., Konig, K. and Andreesen, J. R. Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase. FEMS Microbiology Letters 52 (1988) 13-18.

2. Grether-Beck, S., Igloi, G.L., Pust, S., Schilz, E., Decker, K. and Brandsch, R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13 (1994) 929-936. [PMID: 7815950]

3. Sachelaru, P., Schiltz, E. and Brandsch, R. A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl. Environ. Microbiol. 72 (2006) 5126-5131. [PMID: 16820521]

[EC 1.5.99.14 created 2012]

EC 1.5.99.15

Accepted name: dihydromethanopterin reductase (acceptor)

Reaction: 5,6,7,8-tetrahydromethanopterin + oxidized acceptor = 7,8-dihydromethanopterin + reduced acceptor

For diagram of reaction click here.

Other name(s): DmrX

Systematic name: 5,6,7,8-tetrahydromethanopterin:acceptor 5,6-oxidoreductase

Comments: This archaeal enzyme catalyses the last step in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. The enzyme, characterized from the archaea Methanosarcina mazei and Methanocaldococcus jannaschii, is an iron-sulfur flavoprotein. cf. EC 1.5.1.47, dihydromethanopterin reductase [NAD(P)+].

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

References:

1. Wang, S., Tiongson, J. and Rasche, M.E. Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei. J. Bacteriol. 196 (2014) 203-209. [PMID: 23995635]

[EC 1.5.99.15 created 2014]


Continued with EC 1.6
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