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

Stable Identifier
R-HSA-390224
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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 SCPx in the beta-oxidation of branched-chain fatty acids in vitro, mutations in the protein are associated with elevated levels of pristanic acid in the blood in vivo and the development of neurological defects (Ferdinandusse et al. 2000, 2006).

Literature References
PubMed ID Title Journal Year
10706581 Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method.

Ferdinandusse, S, Denis, S, van Berkel, E, Dacremont, G, Wanders, RJ

J Lipid Res 2000
16685654 Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy

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

Am J Hum Genet 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
propionyl-CoA C2-trimethyltridecanoyltransferase activity of SCP2-1 [peroxisomal matrix]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created