The Enzyme Database

Your query returned 7 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 (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. [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 1.2.3.10      
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, 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 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 1.14.13.93 [(+)-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. [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, 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]
 
 


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