Phosphatidylcholine—sterol O-acyltransferase
In enzymology, a phosphatidylcholine---sterol O-acyltransferase (EC 2.3.1.43) is an enzyme that catalyzes the chemical reaction
| phosphatidylcholine-sterol O-acyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.43 | ||||||||
| CAS no. | 9031-14-5 | ||||||||
| 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 | ||||||||
| |||||||||
- phosphatidylcholine + a sterol 1-acylglycerophosphocholine + a sterol ester
Thus, the two substrates of this enzyme are phosphatidylcholine and sterol, whereas its two products are 1-acylglycerophosphocholine and sterol ester.
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 phosphatidylcholine:sterol O-acyltransferase. Other names in common use include lecithin---cholesterol acyltransferase, phospholipid---cholesterol acyltransferase, LCAT (lecithin-cholesterol acyltransferase), lecithin:cholesterol acyltransferase, and lysolecithin acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
edit- Bartlett K, Keat MJ, Mercer EI (1974). "Biosynthesis of sterol esters in Phycomyces blakesleeanus". Phytochemistry. 13: 1107–1113. doi:10.1016/0031-9422(74)80083-X.
- Buckley JT, Halasa LN, MacIntyre S (1982). "Purification and partial characterization of a bacterial phospholipid: cholesterol acyltransferase". J. Biol. Chem. 257 (6): 3320–5. PMID 7061477.
- Glomset JA (1968). "The plasma lecithins:cholesterol acyltransferase reaction". J. Lipid Res. 9 (2): 155–67. PMID 4868699.
- Vahouny GV, Treadwell CR (1968). "Enzymatic synthesis and hydrolysis of cholesterol esters". Methods. Biochem. Anal. 16: 219–72. doi:10.1002/9780470110348.ch4. PMID 4877146.
