cholesterol + phosphatidylcholine (lecithin) => cholesterol ester + 2-lysophosphatidylcholine (lysolecithin)

Stable Identifier
Reaction [transition]
Homo sapiens
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LCAT activated by apoA-I catalyzes the reaction of cholesterol and phosphatidylcholine to yield cholesterol esterified with a long-chain fatty acid and 2-lysophosphatidylcholine. While this reaction was first studied in vitro using purified proteins in solution, it occurs in vivo on the surfaces of HDL particles where transiently-bound LCAT is activated by HDL-associated apoA-I protein and consumes HDL-associated cholesterol and phosphatidylcholine. The cholesterol ester reaction product is strongly associated with the HDL particle because of its increased hydrophobicity, while the 2-lysophosphatidylcholine product is released from the particle (Fielding et al. 1972 [2 references]; Adimoolam et al. 1998).

Literature References
PubMed ID Title Journal Year
9829992 Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)

Shieh, JJ, Grabbe, E, Jin, L, Adimoolam, S, Jonas, A

J Biol Chem 1998
4335615 A protein cofactor of lecithin:cholesterol acyltransferase

Shore, VG, Fielding, PE, Fielding, CJ

Biochem Biophys Res Commun 1972
4340992 Lecithin: cholesterol acyltransferase: effects of substrate composition upon enzyme activity

Shore, VG, Fielding, PE, Fielding, CJ

Biochim Biophys Acta 1972
Catalyst Activity

phosphatidylcholine-sterol O-acyltransferase activity of LCAT [extracellular region]

This event is regulated
Orthologous Events
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