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
ec00280  Valine, leucine and isoleucine degradation
ec00350  Tyrosine metabolism
ec00380  Tryptophan metabolism
ec00750  Vitamin B6 metabolism
ec00760  Nicotinate and nicotinamide metabolism
ec00830  Retinol metabolism
ec00982  Drug metabolism - cytochrome P450
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00157  aldehyde oxidase
Genes
HSA: 316(AOX1)
PTR: 459863(AOX1)
PPS: 100968717(AOX1)
PON: 100451794(AOX4) 100939468(AOX1)
NLE: 100583419 100583754(AOX1)
MCC: 701024(AOX1) 701502(AOX4) 701613(AOX2)
MCF: 102131116(AOX1) 102134468(AOX2) 102134825(AOX4)
CSAB: 103217611 103217617 103217619
RRO: 104670351 104670357 104670457
RBB: 108531964 108532268 108532294
CJC: 100393665(AOX1) 100394388(AOX2)
MMU: 11761(Aox1) 213043(Aox2) 71724(Aox3) 71872(Aox4)
RNO: 316421(Aox2) 316424(Aox4) 493909(Aox3) 54349(Aox1)
HGL: 101710340 101722324(Aox4) 101722898(Aox1)
OCU: 100008601(AOX1) 100345417(AOX2) 100345675(AOX3) 100354428(AOX4)
CFA: 488467(AOX4) 608849(AOX2)
AML: 100470835(AOX4) 100471086(AOX2) 100474367(AOX1)
FCA: 101085487(AOX1)
PTG: 102949513(AOX1) 102967431
AJU: 106979979(AOX1)
BTA: 338074(AOX1) 518393(AOX4) 531699(AOX2)
CHX: 102171556 102187632(AOX1) 102188176(AOX1)
SSC: 100523701(AOX1) 100525616(AOX2)
OOR: 101285123(AOX1)
DLE: 111171714
PCAD: 102987494 102992680(AOX1)
RSS: 109444972 109455125(AOX1)
DRO: 112307752
MDO: 100016433(AOX2) 100029977(AOX1) 100030014(AOX4) 107648868
OAA: 100092481(AOX1)
GGA: 424071(AOX1) 424072(AOX2)
MGP: 100548803(AOX1) 100549268
CJO: 107316537(AOX1)
NMEL: 110400687(AOX1) 110400690
APLA: 101795737(AOX1)
ACYG: 106039970(AOX1)
TGU: 100217503(AOX1)
LSR: 110484579(AOX1)
SCAN: 103814515(AOX1)
GFR: 102031924(AOX1)
FAB: 101818190(AOX1)
PHI: 102105114(AOX1)
PMAJ: 107207425
CCAE: 111931979(AOX1)
CCW: 104693769(AOX1)
ETL: 114055687 114055700(AOX1)
FPG: 101915658(AOX1)
FCH: 102057814(AOX1)
CLV: 102097486(AOX1)
EGZ: 104130522
NNI: 104010254(AOX1)
ACUN: 113480959
PADL: 103923316(AOX1)
PSS: 102452808(AOX1) 102453236
CPIC: 101949373(AOX1)
PBI: 103048615(AOX1)
PMUR: 107291766(AOX1)
XTR: 100379890(aox1) 100495429(aox1)
DRE: 570457(aox6) 64265(aox5)
IPU: 108259545
PHYP: 113524277
EEE: 113585478
TRU: 101069055(aox1)
LCO: 104937222(aox1)
MZE: 101479847(aox1)
OLA: 101168436(aox1)
XMA: 102223145(aox1)
XCO: 114140277(aox1)
PRET: 103457351(aox1)
NFU: 107384677(aox1)
AOCE: 111570749(aox1)
POV: 109639006 109639051(aox1)
LCF: 108873170(aox1)
HCQ: 109520227(aox1)
BPEC: 110175588(aox1) 110175628
MALB: 109955752(aox1)
ELS: 105022540(aox1)
PKI: 111856671(aox1)
CEL: CELE_B0222.9(gad-3)
CBR: CBG19218
 » show all
Taxonomy
Reference
1  [PMID:16747217]
  Authors
Gordon AH, Green DE, Subrahmanyan V
  Title
Liver aldehyde oxidase.
  Journal
Biochem J 34:764-74 (1940)
Reference
2  [PMID:20985642]
  Authors
KNOX WE
  Title
The quinine-oxidizing enzyme and liver aldehyde oxidase.
  Journal
J Biol Chem 163:699-711 (1946)
Reference
3  [PMID:13201608]
  Authors
MAHLER HR, MACKLER B, GREEN DE.
  Title
Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein.
  Journal
J Biol Chem 210:465-80 (1954)
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 150:585-99 (1972)
DOI:10.1016/0003-9861(72)90078-1
Reference
5  [PMID:8262244]
  Authors
Tomita S, Tsujita M, Ichikawa Y
  Title
Retinal oxidase is identical to aldehyde oxidase.
  Journal
FEBS Lett 336:272-4 (1993)
DOI:10.1016/0014-5793(93)80818-F
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 338:29-34 (1997)
DOI:10.1006/abbi.1996.9774
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 364:264-72 (1999)
DOI:10.1006/abbi.1999.1129
  Sequence
[mmu:11761] [ocu:100008601]
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 229:31-6 (2003)
DOI:10.1016/S0378-1097(03)00781-X
Other DBs
ExplorEnz - The Enzyme Database: 1.2.3.1
IUBMB Enzyme Nomenclature: 1.2.3.1
ExPASy - ENZYME nomenclature database: 1.2.3.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.2.3.1
BRENDA, the Enzyme Database: 1.2.3.1
CAS: 9029-07-6
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