The Enzyme Database

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EC 2.3.1.176     
Accepted name: propanoyl-CoA C-acyltransferase
Reaction: 3α,7α,12α-trihydroxy-5β-cholanoyl-CoA + propanoyl-CoA = CoA + 3α,7α,12α-trihydroxy-24-oxo-5β-cholestanoyl-CoA
For diagram of cholic acid biosynthesis (sidechain), click here
Other name(s): SCP2 (gene name); peroxisomal thiolase 2; sterol carrier protein-χ; SCPχ; PTE-2 (ambiguous); 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; SCPx; 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
Comments: 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 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
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 (1980) 345–348. [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 (1983) 1560–1567. [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 (1994) 19375–19379. [PMID: 8034703]
4.  Seedorf, U., Brysch, P., Engel, T., Schrage, K. and 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 (1994) 21277–21283. [PMID: 8063752]
5.  Wanders, R.J.A., Denis, S., Wouters, F., Wirtz, K.W.A. and Seedorf, U. Sterol carrier protein X (SCPx) is a peroxisomal branched-chain β-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 (1997) 565–569. [PMID: 9245689]
6.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [PMID: 12543708]
[EC 2.3.1.176 created 2005 (EC 2.3.1.154 created 2000, incorporated 2015)]
 
 


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