_EC Aldehyde oxidase. 2 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,840 PDB entries]
EC 1.2.-.- Acting on the aldehyde or oxo group of donors. [511 PDB entries]
EC 1.2.3.- With oxygen as acceptor. [18 PDB entries]
EC Aldehyde oxidase. [2 PDB entries]    

Reaction: An aldehyde + H(2)O + O(2) = a carboxylate + H(2)O(2).

+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Quinoline oxidase. Retinal oxidase.
Cofactor(s): FAD; Iron-sulfur; Mo cation.


Mo cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: 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 Formerly Ec
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 2 PDB entries in enzyme class E.C.

  PDB code Protein
Structure refinement of the aldehyde oxidoreductase from desulfovibrio gigas at 1.28 a
Source: Desulfovibrio gigas. Bacteria
Chain: A (907 residues) CATH domains: 3.90.1170.50 3.30.365.10 3.30.365.10 3.30.365.10 3.30.365.10
Crystal structure of the mouse liver aldehyde oxidase 3 (mao
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: cd1. Organ: liver
Chains: A, B, C, D (1253 residues)
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD