ENZYME entry: EC 1.2.3.1

Accepted Name
Aldehyde oxidase.
Alternative Name(s)
Quinoline oxidase.
Retinal oxidase.
Reaction catalysed
An aldehyde + H(2)O + O(2) <=> a carboxylate + H(2)O(2)
Cofactor(s)
FAD; Iron-sulfur; Mo cation.
Comment(s)
  • 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.
  • 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).
  • Formerly EC 1.2.3.11.
Cross-references
PROSITEPDOC00484
BRENDA1.2.3.1
EC2PDB1.2.3.1
ExplorEnz1.2.3.1
PRIAM enzyme-specific profiles1.2.3.1
KEGG Ligand Database for Enzyme Nomenclature1.2.3.1
IUBMB Enzyme Nomenclature1.2.3.1
IntEnz1.2.3.1
MEDLINEFind literature relating to 1.2.3.1
MetaCyc1.2.3.1
UniProtKB/Swiss-Prot
Q7XH05, ALDO1_ORYSJ;  Q852M1, ALDO2_ORYSJ;  Q852M2, ALDO3_ORYSJ;  
Q69R21, ALDO4_ORYSJ;  P48034, AOXA_BOVIN;  H9TB17, AOXA_CAVPO;  
Q06278, AOXA_HUMAN;  Q5FB27, AOXA_MACFA;  O54754, AOXA_MOUSE;  
P80456, AOXA_RABIT;  Q9Z0U5, AOXA_RAT;  H9TB19, AOXB_CAVPO;  
C4NYZ3, AOXB_MACFA;  Q5SGK3, AOXB_MOUSE;  Q5QE78, AOXB_RAT;  
G3X982, AOXC_MOUSE;  Q5QE80, AOXC_RAT;  H9TB18, AOXD_CAVPO;  
Q3TYQ9, AOXD_MOUSE;  Q5QE79, AOXD_RAT;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.3.-
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