3-ketopristanoyl-CoA + CoASH => 4,8,12-trimethyltridecanoyl-CoA + propionyl-CoA

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
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Peroxisomal SCPx (Non-specific lipid transfer protein; SCP2) catalyzes the reaction of 3-ketopristanoyl-CoA and CoASH to form 4,8,12-trimethyltridecanoyl-CoA and propionyl-CoA. Both intact SCPx and an SCPx fragment corresponding to approximately the 430 aminoterminal residues of the protein are catalytically active in vitro; the latter form may predominate in vivo. Consistent with the role of rat SCPx in the beta-oxidation of branched-chain fatty acids in vitro (Wanders et al. 1997) mutations in the human protein are associated with loss of SCP thiolase activity in cell extracts in vitro, elevated levels of pristanic acid in the blood in vivo and the development of neurological defects (Ferdinandusse et al. 2006).

Literature References
PubMed ID Title Journal Year
16685654 Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy

Duran, M, Dillmann, U, Rusch, H, Reith, W, Denis, S, Wanders, RJA, Kostopoulos, P, Marziniak, M, Overmars, H, Haas, D, Ferdinandusse, S

Am J Hum Genet 2006
9245689 Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes

Wirtz, KW, Denis, S, Wanders, RJA, Seedorf, U, Wouters, F

Biochem Biophys Res Commun 1997
Catalyst Activity

propionyl-CoA C2-trimethyltridecanoyltransferase activity of SCP2-1 [peroxisomal matrix]

Orthologous Events
Cross References
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