EC - Propanoyl-CoA C-acyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
propanoyl-CoA C-acyltransferase
Other names:
peroxisomal thiolase 2
sterol carrier protein-χ
PTE-2 [ambiguous]
sterol carrier protein-X
SCP2 (gene name)
propionyl-CoA C2-trimethyltridecanoyltransferase
3-oxopristanoyl-CoA hydrolase
3-oxopristanoyl-CoA thiolase
peroxisome sterol carrier protein thiolase
sterol carrier protein
oxopristanoyl-CoA thiolase
peroxisomal 3-oxoacyl coenzyme A thiolase
4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA 2-C-4,8,12-trimethyltridecanoyltransferase
Systematic name:
3α,7α,12α-trihydroxy-5β-cholanoyl-CoA:propanoyl-CoA C-acyltransferase



Also acts on dihydroxy-5β-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R') by EC, bile acid-CoA:amino acid N-acyltransferase [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00092
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033814


  1. Pedersen, J.I. and Gustafsson, J.
    Conversion of 3α,7α,12α-trihydroxy-5β-cholestanoic acid into cholic acid by rat liver peroxisomes.
    FEBS Lett. 121: 345-348 (1981). [PMID: 7461136]
  2. Kase, F., Björkhem, I. and Pedersen, J.I.
    Formation of cholic acid from 3α,7α,12α-trihydroxy-5β-cholestanoic acid by rat liver peroxisomes.
    J. Lipid Res. 24: 1560-1567 (1984). [PMID: 6668450]
  3. Falany, C.N., Johnson, M.R., Barnes, S. and Diasio, R.B.
    Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase.
    J. Biol. Chem. 269: 19375-19379 (1994). [PMID: 8034703]
  4. Seedorf, U., Brysch, P., Engel, T., Schrage, K., Assmann, G.
    Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity.
    J. Biol. Chem. 269: 21277-21283 (1994). [PMID: 8063752]
  5. Wanders, R. J., Denis, S., Wouters, F., Wirtz, K. W., Seedorf, U.
    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.
    Biochem. Biophys. Res. Commun. 236: 565-569 (1997). [PMID: 9245689]
  6. Russell, D. W.
    The enzymes, regulation, and genetics of bile acid synthesis.
    Annu. Rev. Biochem. 72: 137-174 (2003). [PMID: 12543708]

[EC created 2005 (EC created 2000, incorporated 2015)]