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, EAWAG-BBD, EXPASY, 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] |
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[EC 1.2.3.1 created 1961, modified 2002, modified 2004, modified 2012] |
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EC
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1.14.13.67
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Transferred entry: | quinine 3-monooxygenase. Now EC 1.14.14.55, quinine 3-monooxygenase
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[EC 1.14.13.67 created 2000, deleted 2017] |
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EC
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1.14.13.157
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Transferred entry: | 1,8-cineole 2-exo-monooxygenase. Now EC 1.14.14.56, 1,8-cineole 2-exo-monooxygenase
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[EC 1.14.13.157 created 2012, deleted 2017] |
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EC |
1.14.14.55 |
Accepted name: |
quinine 3-monooxygenase |
Reaction: |
quinine + [reduced NADPH—hemoprotein reductase] + O2 = 3-hydroxyquinine + [oxidized NADPH—hemoprotein reductase] + H2O |
Glossary: |
quinine = a quinoline alkaloid |
Other name(s): |
CYP3A4 (gene name) |
Systematic name: |
quinine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50812-30-1, 213327-78-7 |
References: |
1. |
Relling, M.V., Evans, R., Dass, C., Desiderio, D.M. and Nemec, J. Human cytochrome P450 metabolism of teniposide and etoposide. J. Pharmacol. Exp. Ther. 261 (1992) 491–496. [PMID: 1578365] |
2. |
Zhang, H., Coville, P.F., Walker, R.J., Miners, J.O., Birkett, D.J. and Wanwimolruk, S. Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br. J. Clin. Pharmacol. 43 (1997) 245–252. [DOI] [PMID: 9088578] |
3. |
Zhao, X.-J., Kawashiro, T. and Ishizaki, T. Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab. Dispos. 26 (1998) 188–191. [PMID: 9456308] |
4. |
Zhao, X.-J., Yokoyama, H., Chiba, K., Wanwimolruk, S. and Ishizaki, T. Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human liver microsomes and nine recombinant human cytochromes P450. J. Pharmacol. Exp. Ther. 279 (1996) 1327–1334. [PMID: 8968357] |
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[EC 1.14.14.55 created 2000 as EC 1.14.13.67, transferred 2017 to EC 1.14.14.55] |
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EC |
1.14.14.56 |
Accepted name: |
1,8-cineole 2-exo-monooxygenase |
Reaction: |
1,8-cineole + [reduced NADPH—hemoprotein reductase] + O2 = 2-exo-hydroxy-1,8-cineole + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of 1,8-cineole catabolism, click here |
Glossary: |
1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-exo-hydroxy-1,8-cineole = (1R,4S,6S)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol |
Other name(s): |
CYP3A4 |
Systematic name: |
1,8-cineole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-exo-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. cf. EC 1.14.14.55, quinine 3-monooxygenase, EC 1.14.14.57, taurochenodeoxycholate 6-hydroxylase and EC 1.14.14.73, albendazole monooxygenase (sulfoxide-forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Miyazawa, M., Shindo, M. and Shimada, T. Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from Eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes. Drug Metab. Dispos. 29 (2001) 200–205. [PMID: 11159812] |
2. |
Miyazawa, M. and Shindo, M. Biotransformation of 1,8-cineole by human liver microsomes. Nat. Prod. Lett. 15 (2001) 49–53. [DOI] [PMID: 11547423] |
3. |
Miyazawa, M., Shindo, M. and Shimada, T. Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes. Xenobiotica 31 (2001) 713–723. [DOI] [PMID: 11695850] |
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[EC 1.14.14.56 created 2012 as EC 1.14.13.157, transferred 2017 to EC 1.14.14.56, modified 2018] |
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