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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.2.3.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.2.3.1

Enzymes and Genes:
aldehyde oxidase Inferred from experiment : AO2 ( Solanum lycopersicum )
aldehyde oxidase Inferred from experiment : AO1 ( Solanum lycopersicum )
aldehyde oxidase Inferred from experiment : AO3 ( Pisum sativum )
aldehyde oxidase Inferred from experiment : AO2 ( Pisum sativum )
aldehyde oxidase Inferred from experiment : AO1 ( Pisum sativum )
aldehyde oxidase Inferred from experiment : AOX1 ( Homo sapiens )

Supersedes EC number: 1.2.3.11

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reactions:
all-trans-retinal + H2O + oxygen → all-trans-retinoate + hydrogen peroxide + H+ (1.2.3.1)

heptanal + oxygen + H2O → heptanoate + hydrogen peroxide + H+ (1.2.3.1)

acetaldehyde + oxygen + H2O → acetate + hydrogen peroxide + H+ (1.2.3.1)

protocatechualdehyde + oxygen + H2O → protocatechuate + hydrogen peroxide + H+ (1.2.3.9)

1-naphthaldehyde + oxygen + H2O → 1-naphthoate + hydrogen peroxide + H+ (1.2.3.9)

cinnamaldehyde + oxygen + H2O → trans-cinnamate + hydrogen peroxide + H+ (1.2.3.9)

benzaldehyde + oxygen + H2O → benzoate + hydrogen peroxide + H+ (1.2.3.9)

Enzyme Commission Primary Name: aldehyde oxidase

Enzyme Commission Synonyms: quinoline oxidase, retinal oxidase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -31.816002 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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 [Krenitsky72, Yoshihara97]. 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) [Tomita93, Huang99a].

Citations: [Gordon40, Mahler54, KNOX46, Uchida03]

Gene-Reaction Schematic: ?

Instance reactions of [an aldehyde + oxygen + H2O → a carboxylate + hydrogen peroxide + H+] (1.2.3.1):
i1: all-trans-retinal + H2O + oxygen → all-trans-retinoate + hydrogen peroxide + H+ (1.2.3.1)

i2: heptanal + oxygen + H2O → heptanoate + hydrogen peroxide + H+ (1.2.3.1)

i3: acetaldehyde + oxygen + H2O → acetate + hydrogen peroxide + H+ (1.2.3.1)

i4: protocatechualdehyde + oxygen + H2O → protocatechuate + hydrogen peroxide + H+ (1.2.3.9)

i5: 1-naphthaldehyde + oxygen + H2O → 1-naphthoate + hydrogen peroxide + H+ (1.2.3.9)

i6: cinnamaldehyde + oxygen + H2O → trans-cinnamate + hydrogen peroxide + H+ (1.2.3.9)

i7: benzaldehyde + oxygen + H2O → benzoate + hydrogen peroxide + H+ (1.2.3.9)

Unification Links: KEGG:R00635 , Rhea:16829

Relationship Links: BRENDA:EC:1.2.3.1 , ENZYME:EC:1.2.3.1 , IUBMB-ExplorEnz:EC:1.2.3.1 , UniProt:RELATED-TO:O23887 , UniProt:RELATED-TO:O23888 , UniProt:RELATED-TO:P93226 , UniProt:RELATED-TO:Q7G9P4 , UniProt:RELATED-TO:Q7G191 , UniProt:RELATED-TO:Q7G192 , UniProt:RELATED-TO:Q7G193 , UniProt:RELATED-TO:Q06278 , UniProt:RELATED-TO:Q46509

Credits:
Revised 16-Sep-2011 by Caspi R , SRI International


References

Gordon40: Gordon AH, Green DE, Subrahmanyan V (1940). "Liver aldehyde oxidase." Biochem J 34(5);764-74. PMID: 16747217

Huang99a: Huang DY, Furukawa A, Ichikawa Y (1999). "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(2);264-72. PMID: 10190983

KNOX46: KNOX WE (1946). "The quinine-oxidizing enzyme and liver aldehyde oxidase." J Biol Chem 163;699-711. PMID: 20985642

Krenitsky72: Krenitsky TA, Neil SM, Elion GB, Hitchings GH (1972). "A comparison of the specificities of xanthine oxidase and aldehyde oxidase." Arch Biochem Biophys 150(2);585-99. PMID: 5044040

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Mahler54: Mahler, HR, Mackler, B, Green, DE (1954). "Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein." J Biol Chem 210(1);465-80. PMID: 13201608

Tomita93: Tomita S, Tsujita M, Ichikawa Y (1993). "Retinal oxidase is identical to aldehyde oxidase." FEBS Lett 336(2);272-4. PMID: 8262244

Uchida03: Uchida H, Kondo D, Yamashita A, Nagaosa Y, Sakurai T, Fujii Y, Fujishiro K, Aisaka K, Uwajima T (2003). "Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690." FEMS Microbiol Lett 229(1);31-6. PMID: 14659539

Yoshihara97: Yoshihara S, Tatsumi K (1997). "Purification and characterization of hepatic aldehyde oxidase in male and female mice." Arch Biochem Biophys 338(1);29-34. PMID: 9015384


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc13.