Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes

J Biol Chem. 1989 May 25;264(15):8636-40.


Microsomal preparations from retinal pigment epithelium carry out phosphatidylcholine synthesis upon incubation with 1-palmitoyllysophosphatidylcholine and fatty acyl-CoA. Phosphatidylcholine synthesized in situ in this manner is an acyl donor for retinyl ester synthesis, demonstrating the existence of lecithin:retinol acyltransferase. Although acyl transfer to retinol is from the 1-position of phosphatidylcholine, the fatty acid in the 2-position is important in substrate recognition. The finding of this novel enzyme activity in retinal pigment epithelial microsomes suggests that phosphatidylcholine is the endogenous acyl donor in CoA-independent retinol esterification observed in these preparations.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyltransferases / metabolism*
  • Animals
  • Cattle
  • Kinetics
  • Lysophosphatidylcholines / isolation & purification
  • Lysophosphatidylcholines / metabolism
  • Microsomes / enzymology*
  • Phosphatidylcholines / biosynthesis
  • Phosphatidylcholines / isolation & purification
  • Pigment Epithelium of Eye / enzymology*
  • Substrate Specificity


  • Lysophosphatidylcholines
  • Phosphatidylcholines
  • Acyltransferases
  • lecithin-retinol acyltransferase