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
Synonyms
(2S)-pristanoyl-CoA + O2 => trans-2,3-dehydropristanoyl-CoA + H2O2 (ACOX2)
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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
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, RJ, Mannaerts, GP

J Biol Chem 1993
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
pristanoyl-CoA oxidase activity of ACOX2:FAD, ACOXL:FAD [peroxisomal matrix]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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