Propionyl-CoA C2-trimethyltridecanoyltransferase
| propionyl-CoA C2-trimethyltridecanoyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.154 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a propionyl-CoA C2-trimethyltridecanoyltransferase (EC 2.3.1.154) is an enzyme that catalyzes the chemical reaction
- 4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA 3-oxopristanoyl-CoA + CoA
Thus, the two substrates of this enzyme are 4,8,12-trimethyltridecanoyl-CoA and propanoyl-CoA, whereas its two products are 3-oxopristanoyl-CoA and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA C2-4,8,12-trimethyltridecanoyltransferase. Other names in common use include 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, and 2-C-4,8,12-trimethyltridecanoyltransferase.
References
[edit]- Seedorf U, Brysch P, Engel T, Schrage K, Assmann G (1994). "Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity". J. Biol. Chem. 269 (33): 21277–83. PMID 8063752.
- Wanders RJ, Denis S, Wouters F, Wirtz KW, Seedorf U (1997). "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" (PDF). Biochem. Biophys. Res. Commun. 236 (3): 565–569. doi:10.1006/bbrc.1997.7007. PMID 9245689.
