The Enzyme Database

Your query returned 15 entries.    printer_iconPrintable version

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, retinal oxidase (formerly EC 1.2.3.11) [5,7].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, 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. [DOI] [PMID: 5044040]
5.  Tomita, S., Tsujita, M. and Ichikawa, Y. Retinal oxidase is identical to aldehyde oxidase. FEBS Lett. 336 (1993) 272–274. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 14659539]
[EC 1.2.3.1 created 1961, modified 2002, modified 2004, modified 2012]
 
 
EC 1.2.3.2      
Transferred entry: xanthine oxidase. Now EC 1.17.3.2, 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, Gene, 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. [DOI] [PMID: 16201755]
[EC 1.2.3.3 created 1961]
 
 
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, Gene, 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. [DOI] [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, Gene, KEGG, MetaCyc, PDB, 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. [DOI] [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, Gene, 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. [PMID: 16660220]
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) 1319–1324. [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) 433–442. [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) 687–693. [PMID: 9489015]
[EC 1.2.3.7 created 1984, modified 2004, modified 2006]
 
 
EC 1.2.3.8     
Accepted name: pyridoxal oxidase
Reaction: pyridoxal + H2O + O2 = 4-pyridoxate + (?)
For diagram of pyridoxal catabolism, click here
Systematic name: pyridoxal:oxygen 4-oxidoreductase
Comments: A molybdenum protein.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, 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, Gene, 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 dehydrogenase (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: vanillate demethylase. 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: 2 4-hydroxyphenylpyruvate + O2 = 2 4-hydroxyphenylacetate + 2 CO2
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Comments: Involved in tyrosine degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, 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 of abscisic acid biosynthesis, click here
Other name(s): abscisic aldehyde oxidase; AAO3; AOd; AOδ
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 1.14.14.137 [(+)-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, Gene, 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. [DOI] [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. [DOI] [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, Gene, KEGG, MetaCyc
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 8557673]
[EC 1.2.3.15 created 2016]
 
 


Data © 2001–2026 IUBMB
Web site © 2005–2026 Andrew McDonald