Continued from EC 1.2.1.51 to EC 1.2.1.82
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 1.2.99 With other acceptors
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, 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 1.2.2.2 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)]
Accepted name: formate dehydrogenase (cytochrome-c-553)
Reaction: formate + ferricytochrome c-553 = CO2 + ferrocytochrome c-553
Systematic name: formate:ferricytochrome-c-553 oxidoreductase
Comments: Yeast cytochrome c, ferricyanide and phenazine methosulfate can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 37251-01-7 (same as EC 1.2.2.1)
References:
1. Yagi, T. Formate: cytochrome oxidoreductase of Desulfovibrio vulgaris. J. Biochem. (Tokyo) 66 (1969) 473-478. [PMID: 4982127]
2. Yagi, T. Purification and properties of cytochrome c-553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, Miyazaki. Biochim. Biophys. Acta 548 (1979) 96-105. [PMID: 226135]
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, 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]
Accepted name: aldehyde oxidase
Reaction: an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Other name(s): quinoline oxidase
Systematic name: aldehyde:oxygen oxidoreductase
Comments: Contains molybdenum, [2Fe-2S] centres and FAD. Also oxidizes quinoline and pyridine derivatives. May be identical with EC 1.2.3.11, retinal oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, 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.
2. Knox, W.E. The quinine-oxidizing enzyme and liver aldehyde oxidase. J. Biol. Chem. 163 (1946) 699-711.
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. 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]
5. 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 1.2.3.2 Transferred entry: now EC 1.1.3.22 xanthine oxidase (EC 1.2.3.2 created 1961, deleted 1984)]
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, GO, KEGG, 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]
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, 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]
Accepted name: glyoxylate oxidase
Reaction: glyoxylate + H2O + O2 = oxalate + H2O2
Systematic name: glyoxylate:oxygen oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, 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)
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, 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]
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, 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.Ê 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) 1319Ð1324. [PMID: 12231908]
6.Ê 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) 433Ð442. [PMID: 9615466]
7.Ê 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) 687Ð693. [PMID: 9489015]
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, 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.
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, 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 1.2.3.10 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)]
Accepted name: retinal oxidase
Reaction: retinal + O2 + H2O = retinoate + H2O2
For diagram of reaction click here.
Other name(s): retinene oxidase
Systematic name: retinal:oxygen oxidoreductase
Comments: May be the same as EC 1.2.3.1, aldehyde oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9033-52-7
References:
1. Mandal, S.K. and Chaudhuri, B.D. Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental thyroid disorders. Indian J. Exp. Biol. 25 (1987) 796-797. [PMID: 3452601]
2. 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]
[EC 1.2.3.12 Transferred entry: now EC 1.14.13.82 vanillate monooxygenase. (EC 1.2.3.12 created 2000, deleted 2003)]
Accepted name: 4-hydroxyphenylpyruvate oxidase
Reaction: 4-hydroxyphenylpyruvate + ½ O2 = 4-hydroxyphenylacetate + CO2
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Comments: Involved in tyrosine degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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, 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]
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 dehydogenase 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, 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]
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, 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 1.2.4.3 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)]
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, 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]
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, 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]
Accepted name: pyruvate synthase
Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives [see also EC 1.2.7.3, 2-oxoglutarate synthase, EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase]
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: 2-oxobutyrate synthase
Reaction: 2-oxobutanoate + CoA + 2 oxidized ferredoxin = propanoyl-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase
Systematic name: 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, CAS registry number: 37251-04-0
References:
1. Buchanan, B.B. Role of ferredoxin in the synthesis of α-ketobutyrate from propionyl coenzyme A and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria. J. Biol. Chem. 244 (1969) 4218-4223. [PMID: 5800441]
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: This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7, , 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase) [3]. Contains thiamine diphosphate and 2 [4Fe-4S] clusters. Highly specific for 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
Accepted name: carbon-monoxide dehydrogenase (ferredoxin)
Reaction: CO + H2O + 2 oxidized ferredoxin = CO2 + reduced ferredoxin + 2 H+
Systematic name: carbon-monoxide,water:ferredoxin oxidoreductase
Comments: Contains nickel, zinc and non-heme iron. Methyl viologen can act as acceptor. The enzyme from Moorella thermoacetica exists as a complex with EC 2.3.1.169, CO-methylating acetyl CoA synthase, which catalyses the overall reaction:
methylcorrinoid protein + CoA + CO2 + reduced ferredoxin = acetyl-CoA + corrinoid protein + H2O + oxidized ferredoxin.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Meyer, O. and Schlegel, H.-G. Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans. J. Bacteriol. 141 (1980) 74-80. [PMID: 7354006]
2.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]
3. 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]
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, 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]
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, 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]
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: This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase; EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase). It 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.
Links to other databases: BRENDA, EXPASY, KEGG, 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]
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: This enzyme, which is found in archaea, is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 2-oxoisovalerate ferredoxin reductase) [4]. 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.
Links to other databases: BRENDA, EXPASY, KEGG, 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 1.2.7.9 Deleted entry: This enzyme is identical to EC 1.2.7.3, 2-oxoglutarate synthase (EC 1.2.7.9 created 2003, deleted 2005)]
Accepted name: oxalate oxidoreductase
Reaction: oxalate + 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, 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]
Accepted name: carbon-monoxide dehydrogenase (acceptor)
Reaction: CO + H2O + A = CO2 + AH2
Other name(s): anaerobic carbon monoxide dehydrogenase; carbon monoxide oxygenase; carbon-monoxide dehydrogenase; carbon-monoxide:(acceptor) oxidoreductase
Systematic name: carbon-monoxide:acceptor oxidoreductase
Comments: Contains a [Ni3Fe-4S] cluster and [4Fe-4S] clusters. It uses many electron acceptors, including ferredoxin, methyl viologen and benzyl viologen and flavins, but not pyridine nucleotides. Forms part of a membrane-bound multienzyme complex with EC 1.12.99.6, hydrogenase (acceptor), which catalyses the overall reaction: CO + H2O = CO2 + H2.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, UM-BBD, CAS registry number: 64972-88-9
References:
1. 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]
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. 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]
4. 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]
Accepted name: aldehyde dehydrogenase (pyrroloquinoline-quinone)
Reaction: an aldehyde + acceptor + H2O = a carboxylate + reduced acceptor
Other name(s): aldehyde dehydrogenase (acceptor)
Systematic name: aldehyde:(pyrroloquinoline-quinone) oxidoreductase
Comments: A quinoprotein. Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 75536-77-5
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]
Accepted name: formaldehyde dismutase
Reaction: 2 formaldehyde = formate + methanol
Other name(s): aldehyde dismutase; cannizzanase
Systematic name: formaldehyde:formaldehyde oxidoreductase
Comments: Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 85204-94-0
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.
Accepted name: formylmethanofuran dehydrogenase
Reaction: formylmethanofuran + H2O + acceptor = CO2 + methanofuran + reduced acceptor
For diagram of reaction click here
Glossary: methanofuran
Other name(s): formylmethanofuran:(acceptor) oxidoreductase
Systematic name: formylmethanofuran:acceptor oxidoreductase
Comments: A molybdoprotein containing a pterin cofactor. Methyl viologen can act as acceptor. Also oxidizes N-furfurylformamide.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, CAS registry number: 119940-12-4
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]
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, 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]
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, 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]