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

Stable Identifier
Reaction [transition]
Homo sapiens
(2S)-pristanoyl-CoA + O2 => trans-2,3-dehydropristanoyl-CoA + H2O2 (ACOX2)
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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

Marynen, P, Vandekerckhove, J, Puype, M, Van Veldhoven, PP, Leunissen, JA, Vanhooren, JC, Mannaerts, GP, Fransen, M, Baumgart, E, Fahimi, HD

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, Denis, S, Van Veldhoven, PP, Wanders, RJ, Eyssen, HJ, Mannaerts, GP, Fransen, M

J Biol Chem 1993
Catalyst Activity

pristanoyl-CoA oxidase activity of ACOX2:FAD, ACOXL:FAD [peroxisomal matrix]

Orthologous Events
Cross References
Cite Us!