Reactome | ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA

ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA

Stable Identifier

R-HSA-389889

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix

Synonyms

(2S)-pristanoyl-CoA + O2 => (2E)-pristenoyl-CoA + H2O2, (2S)-pristanoyl-CoA + O2 => trans-2,3-dehydropristanoyl-CoA + H2O2 (ACOX2)

ReviewStatus

5/5

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ACOX2:FAD, ACOXL:FAD oxidise (2S)-pristanoyl-CoA to trans-2,3-dehydropristanoyl-CoA

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In human liver and kidney tissue, monomeric peroxisomal ACOX2 (bound to FAD cofactor) catalyzes the reaction of (2S)-pristanoyl-CoA and O2 to form trans-2,3-dehydropristanoyl-CoA and H2O2 (Vanhove et al. 1993; Baumgart et al. 1996). A putative acyl-coenzyme A oxidase-like protein ACOXL could catalyse this type of reaction but its activity has not yet been determined.

Literature References

PubMed ID	Title	Journal	Year
8943006	Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome Baumgart, E, Vanhooren, JC, Fransen, M, Marynen, P, Puype, M, Vandekerckhove, J, Leunissen, JA, Fahimi, HD, Mannaerts, GP, Van Veldhoven, PP	Proc Natl Acad Sci U S A	1996
8387517	The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney Vanhove, GF, Van Veldhoven, PP, Fransen, M, Denis, S, Eyssen, HJ, Wanders, RJA, Mannaerts, GP	J Biol Chem	1993