Acyl-CoA oxidase, C-terminal (IPR002655)

Short name: Acyl-CoA_oxidase_C

Overlapping homologous superfamilies

Domain relationships



Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [PMID: 11872165].

Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subunit is folded into the N-terminal alpha-domain, beta-domain, and C-terminal alpha-domain [PMID: 11872165]. Functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments [PMID: 15581893].

Experimental data indicate that, in the pumpkin, the expression pattern of ACOX is very similar to that of the glyoxysomal enzyme 3-ketoacyl-CoA thiolase [PMID: 9525937]. In humans, defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy, also known as peroxisomal acyl-CoA oxidase deficiency. Pseudo-NALD is a peroxisomal single-enzyme disorder. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly and hearing deficit. Pseudo-NALD is characterised by increased plasma levels of very-long chain fatty acids due to a decrease in, or absence of, peroxisome acyl-CoA oxidase activity, despite the peroxisomes being intact and functioning.

This entry represents the Acyl-CoA oxidase C-terminal.

GO terms

Biological Process

GO:0006635 fatty acid beta-oxidation

Molecular Function

GO:0003997 acyl-CoA oxidase activity

Cellular Component

GO:0005777 peroxisome

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.