Enzyme Nomenclature

Continued from EC 1.2.1.51 to EC 1.2.1.99

EC 1.2.2 to EC 1.2.99

Sections

EC 1.2.2 With a cytochrome as acceptor
EC 1.2.3 With oxygen as acceptor
EC 1.2.4 With a disulfide as acceptor
EC 1.2.7 With an iron-sulfur protein as acceptor
EC 1.2.98 With other, known, physiological acceptors

EC 1.2.99 With unknown physiological acceptors


EC 1.2.2 With a cytochrome as acceptor

Contents

EC 1.2.2.1 formate dehydrogenase (cytochrome)
EC 1.2.2.2 deleted covered by EC 1.2.5.1
EC 1.2.2.3 transferred now EC 1.17.2.3
EC 1.2.2.4 carbon-monoxide oxygenase (cytochrome b-561)


EC 1.2.2.1

Accepted name: formate dehydrogenase (cytochrome)

Reaction: formate + 2 ferricytochrome b1 = CO2 + 2 ferrocytochrome b1 + 2 H+

Other name(s): formate dehydrogenase; formate:cytochrome b1 oxidoreductase

Systematic name: formate:ferricytochrome-b1 oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-01-7 (same as EC 1.2.2.3)

References:

1. Gale, E.F. Formic dehydrogenase of Bacterium coli: its inactivation by oxygen and its protection in the bacterial cell. Biochem. J. 33 (1939) 1012-1027.

[EC 1.2.2.1 created 1961]

[EC 1.2.2.2 Deleted entry: pyruvate dehydrogenase (cytochrome). Now covered by EC 1.2.5.1, pyruvate dehydrogenase (quinone) (EC 1.2.2.2 created 1961, deleted 2010)]

[EC 1.2.2.3 Transferred entry: formate dehydrogenase (cytochrome-c-553). Now EC 1.17.2.3, formate dehydrogenase (cytochrome-c-553) (EC 1.2.2.3 created 1981, deleted 2017)]

EC 1.2.2.4

Accepted name: carbon-monoxide dehydrogenase (cytochrome b-561)

Reaction: CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561

Other name(s): carbon monoxide oxidase; carbon monoxide oxygenase (cytochrome b-561); carbon monoxide:methylene blue oxidoreductase; CO dehydrogenase; carbon-monoxide dehydrogenase

Systematic name: carbon monoxide,water:cytochrome b-561 oxidoreductase

Comments: Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 395639-79-9

References:

1. Meyer, O., Jacobitz, S. and Krüger, B. Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria. FEMS Microbiol. Rev. 39 (1986) 161-179.

2. Jacobitz, S. and Meyer, O. Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes and restoration of respiratory activities. J. Bacteriol. 171 (1989) 6294-6299. [PMID: 2808305]

3. Meyer, O. and Schlegel, H.-G. Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans. J. Bacteriol. 141 (1980) 74-80. [PMID: 7354006]

4. Dobbek, H., Gremer, L., Meyer, O. and Huber, R. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc. Natl. Acad. Sci. USA 96 (1999) 8884-8889. [PMID: 10430865]

5. Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and Meyer, O. The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase. J. Mol. Biol. 301 (2000) 1221-1235. [PMID: 10966817]

[EC 1.2.2.4 created 1999 (EC 1.2.3.10 created 1990, incorporated 2003), modified 2003]


EC 1.2.3 With oxygen as acceptor

Contents

EC 1.2.3.1 aldehyde oxidase
EC 1.2.3.2 now EC 1.1.3.22
EC 1.2.3.3 pyruvate oxidase
EC 1.2.3.4 oxalate oxidase
EC 1.2.3.5 glyoxylate oxidase
EC 1.2.3.6 pyruvate oxidase (CoA-acetylating)
EC 1.2.3.7 indole-3-acetaldehyde oxidase
EC 1.2.3.8 pyridoxal oxidase
EC 1.2.3.9 aryl-aldehyde oxidase
EC 1.2.3.10 deleted
EC 1.2.3.11 deleted now included with EC 1.2.3.1
EC 1.2.3.12 vanillate demethylase
EC 1.2.3.12 now EC 1.14.13.82
EC 1.2.3.13 4-hydroxyphenylpyruvate oxidase
EC 1.2.3.14 abscisic aldehyde oxidase
EC 1.2.3.15 (methyl)glyoxal oxidase


EC 1.2.3.1

Accepted name: aldehyde oxidase

Reaction: an aldehyde + H2O + O2 = a carboxylate + H2O2

Other name(s): quinoline oxidase; retinal oxidase

Systematic name: aldehyde:oxygen oxidoreductase

Comments: Contains molybdenum, [2Fe-2S] centres and FAD. The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6]. The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11, retinal oxidase) [5,7].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 9029-07-6

References:

1. Gordon, A.H., Green, D.E. and Subrahmanyan, V. Liver aldehyde oxidase. Biochem. J. 34 (1940) 764-774. [PMID: 16747217]

2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. J. Biol. Chem. 163 (1946) 699-711. [PMID: 20985642]

3. Mahler, H.R., Mackler, B., Green, D.E. and Bock, R.M. Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein. J. Biol. Chem. 210 (1954) 465-480. [PMID: 13201608]

4. Krenitsky, T.A., Neil, S.M., Elion, G.B. and Hitchings, G.H. A comparison of the specificities of xanthine oxidase and aldehyde oxidase. Arch. Biochem. Biophys. 150 (1972) 585-599. [PMID: 5044040]

5. Tomita, S., Tsujita, M. and Ichikawa, Y. Retinal oxidase is identical to aldehyde oxidase. FEBS Lett. 336 (1993) 272-274. [PMID: 8262244]

6. Yoshihara, S. and Tatsumi, K. Purification and characterization of hepatic aldehyde oxidase in male and female mice. Arch. Biochem. Biophys. 338 (1997) 29-34. [PMID: 9015384]

7. Huang, D.-Y., Furukawa, A. and Ichikawa, Y. Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch. Biochem. Biophys. 364 (1999) 264-272. [PMID: 10190983]

8. Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K. and Uwajima, T. Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690. FEMS Microbiol. Lett. 229 (2003) 31-36. [PMID: 14659539]

[EC 1.2.3.1 created 1961, modified 2002, modified 2004, modified 2012]

[EC 1.2.3.2 Transferred entry: now EC 1.1.3.22 xanthine oxidase (EC 1.2.3.2 created 1961, deleted 1984)]

EC 1.2.3.3

Accepted name: pyruvate oxidase

Reaction: pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2

Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium

Other name(s): pyruvic oxidase; phosphate-dependent pyruvate oxidase

Systematic name: pyruvate:oxygen 2-oxidoreductase (phosphorylating)

Comments: A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-96-1

References:

1. Williams, F.R. and Hager, L.P. Crystalline flavin pyruvate oxidase from Escherichia coli. I. Isolation and properties of the flavoprotein. Arch. Biochem. Biophys. 116 (1966) 168-176. [PMID: 5336022]

2. Tittmann, K., Wille, G., Golbik, R., Weidner, A., Ghisla, S. and Hübner, G. Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair. Biochemistry 44 (2005) 13291-13303. [PMID: 16201755]

[EC 1.2.3.3 created 1961, modified 2006]

EC 1.2.3.4

Accepted name: oxalate oxidase

Reaction: oxalate + O2 + 2 H+ = 2 CO2 + H2O2

Other name(s): aero-oxalo dehydrogenase; oxalic acid oxidase

Systematic name: oxalate:oxygen oxidoreductase

Comments: Contains Mn2+ as a cofactor. The enzyme is not a flavoprotein as had been thought [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-79-2

References:

1. Datta, P.K., Meeuse, B.J.D., Engstrom-Heg, V. and Hilal, S.H. Moss oxalic acid oxidase - a flavoprotein. Biochim. Biophys. Acta 17 (1955) 602-603. [PMID: 13250021]

2. Kotsira, V.P. and Clonis, Y.D. Oxalate oxidase from barley roots: purification to homogeneity and study of some molecular, catalytic, and binding properties. Arch. Biochem. Biophys. 340 (1997) 239-249. [PMID: 9143327]

3.Requena, L., and Bornemann, S. Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme. Biochem. J. 343 (1999) 185-190. [PMID: 10493928]

[EC 1.2.3.4 created 1961]

EC 1.2.3.5

Accepted name: glyoxylate oxidase

Reaction: glyoxylate + H2O + O2 = oxalate + H2O2

Systematic name: glyoxylate:oxygen oxidoreductase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-03-9

References:

1. Kasai, T., Suzuki, I. and Asai, T. [Glyoxylic oxidase system in Acetobacter.] Koso Kagaku Shimpojiumu 17 (1962) 77-81. (in Japanese)

[EC 1.2.3.5 created 1972]

EC 1.2.3.6

Accepted name: pyruvate oxidase (CoA-acetylating)

Reaction: pyruvate + CoA + O2 = acetyl-CoA + CO2 + H2O2

Systematic name: pyruvate:oxygen 2-oxidoreductase (CoA-acetylating)

Comments: A flavoprotein (FAD). May be identical with EC 1.2.7.1 pyruvate synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-57-4

References:

1. Reeves, R.E., Warren, L.G., Susskind, B. and Lo, H.-S. An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase. J. Biol. Chem. 252 (1977) 726-731. [PMID: 13076]

2. Takeuchi, T., Weinbach, E.C. and Diamond, L.S. Pyruvate oxidase (CoA acetylating) in Entamoeba histolytica. Biochem. Biophys. Res. Commun. 65 (1975) 591-596. [PMID: 167776]

[EC 1.2.3.6 created 1976]

EC 1.2.3.7

Accepted name: indole-3-acetaldehyde oxidase

Reaction: (indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2

Other name(s): indoleacetaldehyde oxidase; IAAld oxidase; AO1; indole-3-acetaldehyde:oxygen oxidoreductase

Systematic name: (indol-3-yl)acetaldehyde:oxygen oxidoreductase

Comments: A hemoprotein. This enzyme is an isoform of aldehyde oxidase (EC 1.2.3.1). It has a preference for aldehydes having an indole-ring structure as substrate [6,7]. It may play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana [7]. While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly. The enzyme from maize contains FAD, iron and molybdenum [4].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 66082-22-2

References:

1. Bower, P.J., Brown, H.M. and Purves, W.K. Cucumber seedling indoleacetaldehyde oxidase. Plant Physiol. 61 (1978) 107-110.

2. Miyata, S., Suzuki, Y., Kamisaka, S. and Masuda, Y. Indole-3-acetaldehyde oxidase of pea-seedlings. Physiol. Plant. 51 (1981) 402-406.

3. Rajagopal, R. Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles. Physiol. Plant. 24 (1971) 272-281.

4. Koshiba, T., Saito, E., Ono, N., Yamamoto, N. and Sato, M. Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize. Plant Physiol. 110 (1996) 781-789. [PMID: 12226218]

5. Koshiba, T. and Matsuyama, H. An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts. Plant Physiol. 102 (1993) 13191324. [PMID: 12231908]

6. Sekimoto, H., Seo, M., Kawakami, N., Komano, T., Desloire, S., Liotenberg, S., Marion-Poll, A., Caboche, M., Kamiya, Y. and Koshiba, T. Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana. Plant Cell Physiol. 39 (1998) 433442. [PMID: 9615466]

7. Seo, M., Akaba, S., Oritani, T., Delarue, M., Bellini, C., Caboche, M. and Koshiba, T. Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana. Plant Physiol. 116 (1998) 687693. [PMID: 9489015]

[EC 1.2.3.7 created 1984, modified 2004]

EC 1.2.3.8

Accepted name: pyridoxal oxidase

Reaction: pyridoxal + H2O + O2 = 4-pyridoxate + (?)

Systematic name: pyridoxal:oxygen 4-oxidoreductase

Comments: A molybdenum protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 76415-81-1

References:

1. Hanly, E.W. Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila melanogaster. Mol. Gen. Genet. 180 (1980) 455-462.

2. Warner, C.K., Watts, D.T. and Finnerty, V. Molybdenum hydroxylases in Drosophila. I. Preliminary studies of pyridoxal oxidase. Mol. Gen. Genet. 180 (1980) 449-453.

[EC 1.2.3.8 created 1984]

EC 1.2.3.9

Accepted name: aryl-aldehyde oxidase

Reaction: an aromatic aldehyde + O2 + H2O = an aromatic carboxylate + H2O2

Systematic name: aryl-aldehyde:oxygen oxidoreductase

Comments: Acts on benzaldehyde, vanillin and a number of other aromatic aldehydes, but not on aliphatic aldehydes or sugars.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82657-93-0

References:

1. Crawford, D.L., Sutherland, J.B., Pometto, A.L., III and Miller, J.M. Production of an aromatic aldehyde oxidase by Streptomyces viridosporus. Arch. Microbiol. 131 (1982) 351-355.

[EC 1.2.3.9 created 1986, modified 2002]

[EC 1.2.3.10 Deleted entry: carbon-monoxide oxidase. Activity due to EC 1.2.2.4 carbon-monoxide oxygenase (cytochrome b-561). (EC 1.2.3.10 created 1990, deleted 2003)]

[EC 1.2.3.11 Deleted entry: retinal oxidase. Now included with EC 1.2.3.1, aldehyde oxidase (EC 1.2.3.11 created 1990, modified 2002, deleted 2011)]

[EC 1.2.3.12 Transferred entry: now EC 1.14.13.82 vanillate monooxygenase. (EC 1.2.3.12 created 2000, deleted 2003)]

EC 1.2.3.13

Accepted name: 4-hydroxyphenylpyruvate oxidase

Reaction: 4-hydroxyphenylpyruvate + ½ O2 = 4-hydroxyphenylacetate + CO2

For diagram of reaction click here.

Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)

Comments: Involved in tyrosine degradation pathway in Arthrobacter sp.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 78213-74-8

References:

1. Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128-1139. [PMID: 20216]

[EC 1.2.3.13 created 2000]

EC 1.2.3.14

Accepted name: abscisic-aldehyde oxidase

Reaction: abscisic aldehyde + H2O + O2 = abscisate + H2O2

For diagram click here.

Other name(s): abscisic aldehyde oxidase; AAO3; AOd

Systematic name: abscisic-aldehyde:oxygen oxidoreductase

Comments: Acts on both (+)- and (–)-abscisic aldehyde. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, (xanthoxin dehydrogenase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase]. While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 129204-36-0

References:

1. Sagi, M., Fluhr, R. and Lips, S.H. Aldehyde oxidase and xanthin dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype. Plant Physiol. 120 (1999) 571-577. [PMID: 10364409]

2. Seo, M., Peeters, A.J., Koiwai, H., Oritani, T., Marion-Poll, A., Zeevaart, J.A., Koornneef, M., Kamiya, Y. and Koshiba, T. The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves. Proc. Natl. Acad. Sci. USA 97 (2000) 12908-12913. [PMID: 11050171]

3. Seo, M., Koiwai, H., Akaba, S., Komano, T., Oritani, T., Kamiya, Y. and Koshiba, T. Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana. Plant J. 23 (2000) 481-488. [PMID: 10972874]

[EC 1.2.3.14 created 2005]

EC 1.2.3.15

Accepted name: (methyl)glyoxal oxidase

Reaction: (1) glyoxal + H2O + O2 = glyoxylate + H2O2
(2) 2-oxopropanal + H2O + O2 = pyruvate + H2O2

Glossary: 2-oxopropanal = methylglyoxal

Other name(s): glx1 (gene name); glx2 (gene name)

Systematic name: (methyl)glyoxal:oxygen oxidoreductase

Comments: The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis.

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

References:

1. Kersten, P.J. and Kirk, T.K. Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium. J. Bacteriol. 169 (1987) 2195-2201. [PMID: 3553159]

2. Kersten, P.J. and Cullen, D. Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Proc. Natl. Acad. Sci. USA 90 (1993) 7411-7413. [PMID: 8346264]

3. Kersten, P.J., Witek, C., vanden Wymelenberg, A. and Cullen, D. Phanerochaete chrysosporium glyoxal oxidase is encoded by two allelic variants: structure, genomic organization, and heterologous expression of glx1 and glx2. J. Bacteriol. 177 (1995) 6106-6110. [PMID: 7592374]

4. Whittaker, M.M., Kersten, P.J., Nakamura, N., Sanders-Loehr, J., Schweizer, E.S. and Whittaker, J.W. Glyoxal oxidase from Phanerochaete chrysosporium is a new radical-copper oxidase. J. Biol. Chem. 271 (1996) 681-687. [PMID: 8557673]

[EC 1.2.3.15 created 2016]


EC 1.2.4 With a disulfide as acceptor

Contents

EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring)
EC 1.2.4.2 oxoglutarate dehydrogenase (succinyl-transferring)
EC 1.2.4.3 deleted, included in EC 1.2.4.4
EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)


EC 1.2.4.1

Accepted name: pyruvate dehydrogenase (acetyl-transferring)

Reaction: pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2

For diagram of reaction click here.

Glossary: dihydrolipoyl group
thiamine diphosphate

Other name(s): MtPDC (mitochondrial pyruvate dehydrogenase complex); pyruvate decarboxylase; pyruvate dehydrogenase; pyruvate dehydrogenase (lipoamide); pyruvate dehydrogenase complex; pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating); pyruvic acid dehydrogenase; pyruvic dehydrogenase

Systematic name: pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating)

Comments: Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-20-4

References:

1. Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.

2. Scriba, P. and Holzer, H. Gewinnung von αHydroxyäthyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel. Biochem. Z. 334 (1961) 473-486.

3. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]

[EC 1.2.4.1 created 1961, modified 2003]

EC 1.2.4.2

Accepted name: oxoglutarate dehydrogenase (succinyl-transferring)

Reaction: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2

For diagram of reaction click here and for mechanism click here.

Glossary: dihydrolipoyl group
thiamine diphosphate

Other name(s): 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate: lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; αketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase; oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide)

Systematic name: 2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)

Comments: Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9031-02-1

References:

1. Massey, V. The composition of the ketoglutarate dehydrogenase complex. Biochim. Biophys. Acta 38 (1960) 447-460.

2. Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183-270.

3. Sanadi, D.R., Littlefield, J.W. and Bock, R.M. Studies on α-ketoglutaric oxidase. II. Purification and properties. J. Biol. Chem.,197 (1952) 851-862.

4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]

[EC 1.2.4.2 created 1961, modified 1980, modified 1986, modified 2003]

[EC 1.2.4.3 Deleted entry: 2-oxoisocaproate dehydrogenase. Now included with EC 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.3 created 1972, deleted 1978)]

EC 1.2.4.4

Accepted name: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)

Reaction: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2

For diagram of reaction click here.

Glossary: dihydrolipoyl group
thiamine diphosphate

Other name(s):2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α-ketoisocaproate dehydrogenase; α-ketoisocaproic dehydrogenase; α-ketoisocaproic-α-keto-α-methylvaleric dehydrogenase; α-ketoisovalerate dehydrogenase; α-oxoisocaproate dehydrogenase; BCKDH; BCOAD; branched chain keto acid dehydrogenase; branched-chain (-2-oxoacid) dehydrogenase (BCD); branched-chain 2-keto acid dehydrogenase; branched-chain 2-oxo acid dehydrogenase; branched-chain α-keto acid dehydrogenase; branched-chain α-oxo acid dehydrogenase; branched-chain keto acid dehydrogenase; branched-chain ketoacid dehydrogenase; dehydrogenase, 2-oxoisovalerate (lipoate); dehydrogenase, branched chain α-keto acid

Systematic name: 3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)

Comments: Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9082-72-8

References:

1. Bowden, J.A. and Connelly, J.L. Branched chain α-keto acid metabolism. II. Evidence for the common identity of α-ketoisocaproic acid and α-keto-β-methyl-valeric acid dehydrogenases. J. Biol. Chem. 243 (1968) 3526-3531. [PMID: 5656388]

2.Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α-ketoisocaproic:α-keto-β-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198-1203. [PMID: 5689906]

3. Danner, D.J., Lemmon, S.K., Beharse, J.C. and Elsas, L.J., II, Purification and characterization of branched chain α-ketoacid dehydrogenase from bovine liver mitochondria. J. Biol. Chem., 254, (1979) 5522-5526. [PMID: 447664]

4. Pettit, F.H., Yeaman, S.J. and Reed, L.J. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA, 75, (1978) 4881-4885. [PMID: 283398]

5. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem., 69, (2000) 961-1004. [PMID: 10966480]

[EC 1.2.4.4 created 1972 (EC 1.2.4.3 created 1972, incorporated 1978), modified 2003]


EC 1.2.5 With a quinone or similar compound as acceptor

Contents

EC 1.2.5.1 pyruvate dehydrogenase (quinone)
EC 1.2.5.2 aldehyde dehydrogenase (quinone)
EC 1.2.5.3 aerobic carbon monoxide dehydrogenase

EC 1.2.5.1

Accepted name: pyruvate dehydrogenase (quinone)

Reaction: pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol

Other name(s): pyruvate dehydrogenase; pyruvic dehydrogenase; pyruvic (cytochrome b1) dehydrogenase; pyruvate:ubiquinone-8-oxidoreductase; pyruvate oxidase (ambiguous); pyruvate dehydrogenase (cytochrome) (incorrect)

Systematic name: pyruvate:ubiquinone oxidoreductase

Comments: Flavoprotein (FAD) [1]. This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone [2,3]. Does not accept menaquinone. Activity is greatly enhanced by lipids [4,5,6]. Requires thiamine diphosphate [7]. The enzyme can also form acetoin [8].

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

References:

1. Recny, M.A. and Hager, L.P. Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD. J. Biol. Chem. 257 (1982) 12878-12886. [PMID: 6752142]

2. Cunningham, C.C. and Hager, L.P. Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids. J. Biol. Chem. 250 (1975) 7139-7146. [PMID: 1100621]

3. Koland, J.G., Miller, M.J. and Gennis, R.B. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry 23 (1984) 445-453. [PMID: 6367818]

4. Grabau, C. and Cronan, J.E., Jr. In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site. Biochemistry 25 (1986) 3748-3751. [PMID: 3527254]

5. Wang, A.Y., Chang, Y.Y. and Cronan, J.E., Jr. Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding. J. Biol. Chem. 266 (1991) 10959-10966. [PMID: 2040613]

6. Chang, Y.Y. and Cronan, J.E., Jr. Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase. Biochemistry 36 (1997) 11564-11573. [PMID: 9305946]

7. O'Brien, T.A., Schrock, H.L., Russell, P., Blake, R., 2nd and Gennis, R.B. Preparation of Escherichia coli pyruvate oxidase utilizing a thiamine pyrophosphate affinity column. Biochim. Biophys. Acta 452 (1976) 13-29. [PMID: 791368]

8. Bertagnolli, B.L. and Hager, L.P. Role of flavin in acetoin production by two bacterial pyruvate oxidases. Arch. Biochem. Biophys. 300 (1993) 364-371. [PMID: 8424670]

[EC 1.2.5.1 created 2010]

EC 1.2.5.2

Accepted name: aldehyde dehydrogenase (quinone)

Reaction: an aldehyde + a quinone + H2O = a carboxylate + a quinol

Other name(s): aldehyde dehydrogenase (acceptor)

Systematic name: aldehyde:quinone oxidoreductase

Comments: Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. The enzymes contains a PQQ cofactor and multiple hemes that deliver the electrons to the membrane quinone pool.

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

References:

1. Ameyama, M. and Adachi, O. Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol. 89 (1982) 491-497.

2. Ameyama, M., Osada, K., Shinagawa, E., Matsushita, K. and Adachi, O. Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti. Agric. Biol. Chem. 45 (1981) 1189-1890.

3. Patel, R.N., Hou, C.T., Derelanko, P. and Felix, A. Purification and properties of a heme-containing aldehyde dehydrogenase from Methylosinus trichosporium. Arch. Biochem. Biophys. 203 (1980) 654-662. [PMID: 6779711]

4. Gomez-Manzo, S., Chavez-Pacheco, J.L., Contreras-Zentella, M., Sosa-Torres, M.E., Arreguin-Espinosa, R., Perez de la Mora, M., Membrillo-Hernandez, J. and Escamilla, J.E. Molecular and catalytic properties of the aldehyde dehydrogenase of Gluconacetobacter diazotrophicus, a quinoheme protein containing pyrroloquinoline quinone, cytochrome b, and cytochrome c. J. Bacteriol. 192 (2010) 5718-5724. [PMID: 20802042]

[EC 1.2.5.2 created 1983 as EC 1.2.99.3, modified 1989, transferred 2015 to EC 1.2.5.2 ]

EC 1.2.5.3

Accepted name: aerobic carbon monoxide dehydrogenase

Reaction: CO + a quinone + H2O = CO2 + a quinol

Other name(s): MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase

Systematic name: carbon-monoxide:quinone oxidoreductase

Comments: This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor [5]. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase.

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

References:

1. Gremer, L., Kellner, S., Dobbek, H., Huber, R. and Meyer, O. Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli, J. Biol. Chem. 275 (2000) 1864-1872. [PMID: 10636886]

2. Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R. and Meyer, O. Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl. Acad. Sci. USA 99 (2002) 15971-15976. [PMID: 12475995]

3. Gnida, M., Ferner, R., Gremer, L., Meyer, O. and Meyer-Klaucke, W. A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy. Biochemistry 42 (2003) 222-230. [PMID: 12515558]

4. Resch, M., Dobbek, H. and Meyer, O. Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans, J. Biol. Inorg. Chem. 10 (2005) 518-528. [PMID: 16091936]

5. Wilcoxen, J., Zhang, B. and Hille, R. Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans with quinones. Biochemistry 50 (2011) 1910-1916. [PMID: 21275368]

6. Pelzmann, A.M., Mickoleit, F. and Meyer, O. Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans, J. Biol. Inorg. Chem. 19 (2014) 1399-1414. [PMID: 25377894]

7. Hille, R., Dingwall, S. and Wilcoxen, J. The aerobic CO dehydrogenase from Oligotropha carboxidovorans, J. Biol. Inorg. Chem. 20 (2015) 243-251. [PMID: 25156151]

[EC 1.2.5.3 created 2016]


EC 1.2.7 With an iron-sulfur protein as acceptor

Contents

EC 1.2.7.1 pyruvate synthase
EC 1.2.7.2 deleted now covered by EC 1.2.7.1
EC 1.2.7.3 2-oxoglutarate synthase
EC 1.2.7.4 anaerobic carbon-monoxide dehydrogenase
EC 1.2.7.5 aldehyde ferredoxin oxidoreductase
EC 1.2.7.6 glyceraldehyde-3-phosphate ferredoxin reductase
EC 1.2.7.7 2-oxoisovalerate ferredoxin reductase
EC 1.2.7.8 indolepyruvate ferredoxin oxidoreductase
EC 1.2.7.9 2-oxoglutarate ferredoxin oxidoreductase
EC 1.2.7.9 deleted, identical to EC 1.2.7.3
EC 1.2.7.10 oxalate oxidoreductase
EC 1.2.7.11 2-oxoacid oxidoreductase (ferredoxin)
EC 1.2.7.12 formylmethanofuran dehydrogenase


EC 1.2.7.1

Accepted name: pyruvate synthase

Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+

For diagram of reaction click here.

Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase; 2-oxobutyrate synthase; α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase; 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating); 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)

Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)

Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).

Links to other databases: BRENDA, EXPASY, KEGG, PDB, Metacyc, CAS registry number: 9082-51-3

References:

1. Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420-1425. [PMID: 5217644]

2. Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963-6969. [PMID: 4628267]

3. Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111-3119. [PMID: 5574389]

4. Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120-3125. [PMID: 4324891]

5. Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663-669. [PMID: 10607667]

[EC 1.2.7.1 created 1972, modified 2003, modified 2013]

[EC 1.2.7.2 Deleted entry: 2-oxobutyrate synthase. Now included with EC 1.2.7.1, pyruvate synthase. (EC 1.2.7.2 created 1972, deleted 2013)]

EC 1.2.7.3

Accepted name: 2-oxoglutarate synthase

Reaction: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+

Other name(s): 2-ketoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR; 2-oxoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating)

Systematic name: 2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating)

Comments: The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37251-05-1

References:

1. Buchanan, B.B. and Evans, M.C.W. The synthesis of α-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 54 (1965) 1212-1218. [PMID: 4286833]

2. Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963-6969. [PMID: 4628267]

3. Dorner, E. and Boll, M. Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring. J. Bacteriol. 184 (2002) 3975-3983. [PMID: 12081970]

4. Mai, X. and Adams, M.W. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 178 (1996) 5890-5896. [PMID: 8830683]

5. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]

[EC 1.2.7.3 created 1972, modified 2005]

EC 1.2.7.4

Accepted name: anaerobic carbon-monoxide dehydrogenase

Reaction: CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+

Other name(s): Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin)

Systematic name: carbon-monoxide,water:ferredoxin oxidoreductase

Comments: This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase.

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

References:

1. Ragsdale, S.W., Clark, J.E., Ljungdahl, L.G., Lundie, L.L. and Drake, H.L. Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein. J. Biol. Chem. 258 (1983) 2364-2369. [PMID: 6687389]

2. Diekert, G. and Ritter, M. Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum, FEBS Lett. 151 (1983) 41-44. [PMID: 6687458]

3. Bonam, D. and Ludden, P.W. Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum, J. Biol. Chem. 262 (1987) 2980-2987. [PMID: 3029096]

4. Drennan, C.L., Heo, J., Sintchak, M.D., Schreiter, E. and Ludden, P.W. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. USA 98 (2001) 11973-11978. [PMID: 11593006]

5. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 293 (2001) 1281-1285. [PMID: 11509720]

6. Doukov, T.I., Iverson, T., Seravalli, J., Ragsdale, S.W. and Drennan, C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567-572. [PMID: 12386327]

7. Can, M., Armstrong, F.A. and Ragsdale, S.W. Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase. Chem. Rev. 114 (2014) 4149-4174. [PMID: 24521136]

[EC 1.2.7.4 created 2003 (EC 1.2.99.2 created 1982, modified 1990, modified 2003, incorporated 2015), modified 2016]

EC 1.2.7.5

Accepted name: aldehyde ferredoxin oxidoreductase

Reaction: an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin

Other name(s): AOR

Systematic name: aldehyde:ferredoxin oxidoreductase

Comments: This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate [see EC 1.2.7.6, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 138066-90-7

References:

1. Mukund, S. and Adams, M.W.W. The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase - evidence for its participation in a unique glycolytic pathway. J. Biol. Chem. 266 (1991) 14208-14216. [PMID: 1907273]

2. Johnson, J.L., Rajagopalan, K.V., Mukund, S. and Adams, M.W.W. Identification of molybdopterin as the organic-component of the tungsten cofactor in four enzymes from hyperthermophilic archaea. J. Biol. Chem. 268 (1993) 4848-4852. [PMID: 8444863]

3. Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W.W. and Rees, D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 (1995) 1463-1469. [PMID: 7878465]

4. Roy, R., Menon, A.L. and Adams, M.W.W. Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331 (2001) 132-144. [PMID: 11265456]

[EC 1.2.7.5 created 2003]

EC 1.2.7.6

Accepted name: glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)

Reaction: D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin

Other name(s): GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase

Systematic name: D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase

Comments: Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 162995-20-2

References:

1. Mukund, S. and Adams, M.W.W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270 (1995) 8389-8392. [PMID: 7721730]

2. Roy, R., Menon, A.L. and Adams, M.W.W. Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331 (2001) 132-144. [PMID: 11265456]

[EC 1.2.7.6 created 2003]

EC 1.2.7.7

Accepted name: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)

Reaction: 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+

Other name(s): 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase

Systematic name: 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)

Comments: The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase.

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

References:

1. Heider, J., Mai, X.H. and Adams, M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 178 (1996) 780-787. [PMID: 8550513]

2. Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862-868. [PMID: 9108258]

3. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]

[EC 1.2.7.7 created 2003]

EC 1.2.7.8

Accepted name: indolepyruvate ferredoxin oxidoreductase

Reaction: (indol-3-yl)pyruvate + CoA + b>2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+

Other name(s):3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR

Systematic name: 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)

Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 158886-06-7

References:

1. Mai, X.H. and Adams, M.W.W. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus - a new enzyme involved in peptide fermentation. J. Biol. Chem. 269 (1994) 16726-16732. [PMID: 8206994]

2. Siddiqui, M.A., Fujiwara, S. and Imanaka, T. Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. K0d1 possesses a mosaic: Structure showing features of various oxidoreductases. Mol. Gen. Genet. 254 (1997) 433-439. [PMID: 9180697]

3. Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862-868. [PMID: 9108258]

4. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]

[EC 1.2.7.8 created 2003]

[EC 1.2.7.9 Deleted entry: This enzyme is identical to EC 1.2.7.3, 2-oxoglutarate synthase (EC 1.2.7.9 created 2003, deleted 2005)]

EC 1.2.7.10

Accepted name: oxalate oxidoreductase

Reaction: oxalate + oxidized ferredoxin = 2 CO2 + reduced ferredoxin

Systematic name: oxalate:ferredoxin oxidoreductase

Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4)

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

References:

1. Daniel, S.L., Pilsl, C. and Drake, H.L. Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica. FEMS Microbiol. Lett. 231 (2004) 39-43. [PMID: 14769464]

2. Pierce, E., Becker, D.F. and Ragsdale, S.W. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. J. Biol. Chem. 285 (2010) 40515-40524. [PMID: 20956531]

[EC 1.2.7.10 created 2011]

EC 1.2.7.11

Accepted name: 2-oxoacid oxidoreductase (ferredoxin)

Reaction: a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+

Other name(s): OFOR

Systematic name: 2-oxocarboxylate:ferredoxin 2-oxidoreductase (decarboxylating, CoA-acylating)

Comments: Contains thiamine diphosphate and [4Fe-4S] clusters [2]. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For example, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).

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

References:

1. Kerscher, L. and Oesterhelt, D. Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium. Eur. J. Biochem. 116 (1981) 587-594. [PMID: 6266826]

2. Zhang, Q., Iwasaki, T., Wakagi, T. and Oshima, T. 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biochem. 120 (1996) 587-599. [PMID: 8902625]

3. Fukuda, E., Kino, H., Matsuzawa, H. and Wakagi, T. Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes. Eur. J. Biochem. 268 (2001) 5639-5646. [PMID: 11683888]

4. Fukuda, E. and Wakagi, T. Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7. Biochim. Biophys. Acta 1597 (2002) 74-80. [PMID: 12009405]

5. Nishizawa, Y., Yabuki, T., Fukuda, E. and Wakagi, T. Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1. FEBS Lett 579 (2005) 2319-2322. [PMID: 15848165]

6. Park, Y.J., Yoo, C.B., Choi, S.Y. and Lee, H.B. Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1. J. Biochem. Mol. Biol. 39 (2006) 46-54. [PMID: 16466637]

[EC 1.2.7.11 created 2013]

EC 1.2.7.12

Accepted name: formylmethanofuran dehydrogenase

Reaction: a formylmethanofuran + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster = CO2 + a methanofuran + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

For diagram of reaction click here.

Glossary: methanofuran a = 4-[4-(2-{[(4R*,5S*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furan-2-ylmethanamine

Other name(s): formylmethanofuran:acceptor oxidoreductase

Systematic name: formylmethanofuran:ferredoxin oxidoreductase

Comments: Contains a molybdopterin cofactor. In some organisms an additional subunit enables the incorporation of tungsten when molybdenum availability is low. The enzyme catalyses a reversible reaction in methanogenic archaea, and is involved in methanogenesis from CO2 as well as the oxidation of coenzyme M to CO2. The reaction is endergonic, and is driven by coupling with the soluble CoB-CoM heterodisulfide reductase via electron bifurcation.

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

References:

1. Karrasch, M., Börner, G., Enssle, M. and Thauer, R.K. The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor. Eur. J. Biochem. 194 (1990) 367-372. [PMID: 2125267]

2. Bertram, P.A., Schmitz, R.A., Linder, D. and Thauer, R.K. Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. Arch. Microbiol. 161 (1994) 220-228. [PMID: 8161283]

3. Bertram, P.A., Karrasch, M., Schmitz, R.A., Bocher, R., Albracht, S.P. and Thauer, R.K. Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. Eur. J. Biochem. 220 (1994) 477-484. [PMID: 8125106]

4. Vorholt, J.A. and Thauer, R.K. The active species of ‘CO2’ utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 248 (1997) 919-924. [PMID: 9342247]

5. Meuer, J., Kuettner, H.C., Zhang, J.K., Hedderich, R. and Metcalf, W.W. Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl Acad. Sci. USA 99 (2002) 5632-5637. [PMID: 11929975]

6. Kaster, A.K., Moll, J., Parey, K. and Thauer, R.K. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl Acad. Sci. USA 108 (2011) 2981-2986. [PMID: 21262829]

[EC 1.2.7.12 created 1992 as EC 1.2.99.5, transferred 2017 to EC 1.2.7.12]


EC 1.2.98 With other, known, physiological acceptors

EC 1.2.98.1

Accepted name: formaldehyde dismutase

Reaction: 2 formaldehyde + H2O = formate + methanol

Other name(s): aldehyde dismutase; cannizzanase; nicotinoprotein aldehyde dismutase

Systematic name: formaldehyde:formaldehyde oxidoreductase

Comments: The enzyme contains a tightly but noncovalently bound NADP(H) cofactor, as well as Zn2+ and Mg2+. Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP+ by reaction with a second formaldehyde, yielding methanol. The enzyme from the bacterium Mycobacterium sp. DSM 3803 also catalyses the reactions of EC 1.1.99.36, alcohol dehydrogenase (nicotinoprotein) and EC 1.1.99.37, methanol dehydrogenase (nicotinoprotein) [3]. Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors [1,2].

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

References:

1. Kato, N., Shirakawa, K., Kobayashi, H. and Sakazawa, C. The dismutation of aldehydes by a bacterial enzyme. Agric. Biol. Chem. 47 (1983) 39-46.

2. Kato, N., Yamagami, T., Shimao, M. and Sakazawa, C. Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur. J. Biochem. 156 (1986) 59-64. [PMID: 3514215]

3. Park, H., Lee, H., Ro, Y.T. and Kim, Y.M. Identification and functional characterization of a gene for the methanol : N,N'-dimethyl-4-nitrosoaniline oxidoreductase from Mycobacterium sp. strain JC1 (DSM 3803). Microbiology 156 (2010) 463-471. [PMID: 19875438]

[EC 1.2.98.1 created 1986 as EC 1.2.99.4, modified 2012, transferred 2015 to EC 1.2.98.1]


EC 1.2.99 With unknown physiological acceptors

Contents

EC 1.2.99.1 now EC EC 1.17.99.4
EC 1.2.99.2 now EC 1.2.7.4
EC 1.2.99.3 aldehyde dehydrogenase (pyrroloquinoline-quinone)
EC 1.2.99.4 now EC 1.2.98.1
EC 1.2.99.5 transferred, now EC 1.2.7.12
EC 1.2.99.6 carboxylate reductase
EC 1.2.99.7 aldehyde dehydrogenase (FAD-independent)
EC 1.2.99.8 glyceraldehyde dehydrogenase (FAD-containing)
EC 1.2.99.9 transferred now EC 1.17.98.3


[EC 1.2.99.1 Transferred entry: now EC 1.17.99.4, uracil/thymine dehydrogenase (EC 1.2.99.1 created 1961, deleted 1984)]

[EC 1.2.99.2 Transferred entry: carbon-monoxide dehydrogenase (acceptor). Now EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.99.2 created 1982, modified 1990, modified 2003, deleted 2016)]

[EC 1.2.99.3 Transferred entry: aldehyde dehydrogenase (pyrroloquinoline-quinone). Now EC 1.2.5.2, aldehyde dehydrogenase (quinone) (EC 1.2.99.3 created 1983, modified 1989, deleted 2014)]

[EC 1.2.99.4 Transferred entry: formaldehyde dismutase. Now EC 1.2.98.1, formaldehyde dismutase. (EC 1.2.99.4 created 1986, modified 2012, deleted 2015)]

[EC 1.2.99.5 Transferred entry: formylmethanofuran dehydrogenase. Now EC 1.2.7.12, formylmethanofuran dehydrogenase (EC 1.2.99.5 created 1992, deleted 2017)]

EC 1.2.99.6

Accepted name: carboxylate reductase

Reaction: an aldehyde + acceptor + H2O = a carboxylate + reduced acceptor

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

Systematic name: aldehyde:acceptor oxidoreductase

Comments: A tungsten protein. Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 125008-36-8

References:

1. White, H., Strobl, G., Feicht, R. and Simon, H. Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. Eur. J. Biochem. 184 (1989) 89-96. [PMID: 2550230]

[EC 1.2.99.6 created 1992]

EC 1.2.99.7

Accepted name: aldehyde dehydrogenase (FAD-independent)

Reaction: an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor

Other name(s): aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd

Systematic name: aldehyde:acceptor oxidoreductase (FAD-independent)

Comments: Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD.

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

References:

1. Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K. and Uwajima, T. Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690. FEMS Microbiol. Lett. 229 (2003) 31-36. [PMID: 14659539]

2. Duarte, R.O., Archer, M., Dias, J.M., Bursakov, S., Huber, R., Moura, I., Romao, M.J. and Moura, J.J. Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774. Biochem. Biophys. Res. Commun. 268 (2000) 745-749. [PMID: 10679276]

3. Andrade, S.L., Brondino, C.D., Feio, M.J., Moura, I. and Moura, J.J. Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491. EPR assignment of the proximal [2Fe-2S] cluster to the Mo site. Eur. J. Biochem. 267 (2000) 2054-2061. [PMID: 10727945]

4. Romao, M.J., Archer, M., Moura, I., Moura, J.J., LeGall, J., Engh, R., Schneider, M., Hof, P. and Huber, R. Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science 270 (1995) 1170-1176. [PMID: 7502041]

[EC 1.2.99.7 created 2004]

EC 1.2.99.8

Accepted name: glyceraldehyde dehydrogenase (FAD-containing)

Reaction: D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor

For diagram of reaction click here.

Other name(s): glyceraldehyde oxidoreductase

Systematic name: D-glyceraldehyde:acceptor oxidoreductase (FAD-containing)

Comments: The enzyme from the archaeon Sulfolobus acidocaldarius catalyses the oxidation of D-glyceraldehyde in the nonphosphorylative Entner-Doudoroff pathway. With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo. The iron-sulfur protein contains FAD and molybdopterin guanine dinucleotide.

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

References:

1. Kardinahl, S., Schmidt, C.L., Hansen, T., Anemuller, S., Petersen, A. and Schafer, G. The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme—an aldehyde oxidoreductase. Eur. J. Biochem. 260 (1999) 540-548. [PMID: 10095793]

[EC 1.2.99.8 created 2013]

[EC 1.2.99.9 Transferred entry: formate dehydrogenase (coenzyme F420). Now EC 1.17.98.3, formate dehydrogenase (coenzyme F420) (EC 1.2.99.9 created 2014, deleted 2017)]


Continued with EC 1.3.1.1 to EC 1.3.1.50
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