KEGG   ENZYME: 1.2.3.1Help
Entry
EC 1.2.3.1                  Enzyme                                 

Name
aldehyde oxidase;
quinoline oxidase;
retinal oxidase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
aldehyde:oxygen oxidoreductase
Reaction(IUBMB)
an aldehyde + H2O + O2 = a carboxylate + H2O2 [RN:R00635]
Reaction(KEGG)
Substrate
aldehyde [CPD:C00071];
H2O [CPD:C00001];
O2 [CPD:C00007]
Product
carboxylate [CPD:C00060];
H2O2 [CPD:C00027]
Comment
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].
History
EC 1.2.3.1 created 1961, modified 2002, modified 2004, modified 2012
Pathway
Valine, leucine and isoleucine degradation
Tyrosine metabolism
Tryptophan metabolism
Vitamin B6 metabolism
Nicotinate and nicotinamide metabolism
Retinol metabolism
Drug metabolism - cytochrome P450
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K00157  
aldehyde oxidase
Genes
HSA: 
316(AOX1)
PPS: 
PON: 
100172665(AOX1)
MCC: 
701024(AOX1) 701502(AOX1) 701613(AOX3L1)
MCF: 
102131116(AOX1) 102134468(AOX1)
MMU: 
11761(Aox1) 213043(Aox2) 71724(Aox3) 71872(Aox4)
RNO: 
316421(Aox2) 316424(Aox4) 493909(Aox3) 54349(Aox1)
CGE: 
HGL: 
TUP: 
CFA: 
488467(AOH2) 608849(AOH3)
AML: 
FCA: 
BTA: 
338074(AOX1) 518393(AOX4) 531699(AOX3L1)
BOM: 
PHD: 
CHX: 
SSC: 
CFR: 
ECB: 
MYB: 
MDO: 
SHR: 
GGA: 
424071(AOX1) 424072(AOX2P)
MGP: 
TGU: 
100217503(AOX1)
FAB: 
101818190(AOX1)
PHI: 
102105114(AOX1)
APLA: 
101795737(AOX1)
FPG: 
101915658(AOX1)
FCH: 
102057814(AOX1)
CLV: 
102097486(AOX1)
ASN: 
PSS: 
ACS: 
XLA: 
444490(aox1)
XTR: 
DRE: 
570457(aox1) 64265(aox3)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102354789(AOX1)
 » show all
Taxonomy
Reference
1  [PMID:16747217]
  Authors
Gordon AH, Green DE, Subrahmanyan V
  Title
Liver aldehyde oxidase.
  Journal
Biochem. J. 34 (1940) 764-74.
Reference
2  [PMID:20985642]
  Authors
KNOX WE
  Title
The quinine-oxidizing enzyme and liver aldehyde oxidase.
  Journal
J. Biol. Chem. 163 (1946) 699-711.
Reference
3  [PMID:13201608]
  Authors
MAHLER HR, MACKLER B, GREEN DE.
  Title
Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein.
  Journal
J. Biol. Chem. 210 (1954) 465-80.
  Organism
Sus scofa [GN:ssc]
Reference
4  [PMID:5044040]
  Authors
Krenitsky TA, Neil SM, Elion GB, Hitchings GH
  Title
A comparison of the specificities of xanthine oxidase and aldehyde oxidase.
  Journal
Arch. Biochem. Biophys. 150 (1972) 585-99.
Reference
5  [PMID:8262244]
  Authors
Tomita S, Tsujita M, Ichikawa Y
  Title
Retinal oxidase is identical to aldehyde oxidase.
  Journal
FEBS. Lett. 336 (1993) 272-4.
Reference
6  [PMID:9015384]
  Authors
Yoshihara S, Tatsumi K
  Title
Purification and characterization of hepatic aldehyde oxidase in male and female  mice.
  Journal
Arch. Biochem. Biophys. 338 (1997) 29-34.
Reference
7  [PMID:10190983]
  Authors
Huang DY, Furukawa A, Ichikawa Y.
  Title
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.
  Journal
Arch. Biochem. Biophys. 364 (1999) 264-72.
  Organism
Mus musculus [GN:mmu], Oryctolagus cuniculus
  Sequence
[mmu:11761]
Reference
8  [PMID:14659539]
  Authors
Uchida H, Kondo D, Yamashita A, Nagaosa Y, Sakurai T, Fujii Y, Fujishiro K, Aisaka K, Uwajima T.
  Title
Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690.
  Journal
FEMS. Microbiol. Lett. 229 (2003) 31-6.
  Organism
Pseudomonas sp.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9029-07-6

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