EC - Phosphatidylcholine—retinol O-acyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
phosphatidylcholine—retinol O-acyltransferase
Other names:
lecithin—retinol acyltransferase
phosphatidylcholine:retinol-(cellular-retinol-binding-protein) O-acyltransferase
lecithin:retinol acyltransferase
lecithin-retinol acyltransferase
retinyl ester synthase
lecithin retinol acyl transferase
Systematic name:
phosphatidylcholine:retinol—[cellular-retinol-binding-protein] O-acyltransferase



A key enzyme in retinoid metabolism, catalysing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. Can also esterify 11-cis-retinol.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102279 , GO:0047173
CAS Registry Number: 117444-03-8


  1. MacDonald, P.N. and Ong, D.E.
    Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine.
    J. Biol. Chem. 263 : 12478-12482 (1988). [PMID: 3410848]
  2. Saari, J.C. and Bredberg, D.L.
    Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes.
    J. Biol. Chem. 264 : 8636-8340 (1989). [PMID: 2722792]
  3. Saari, J. C., Bredberg, D. L., Farrell, D. F.
    Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase.
    Biochem. J. 291 : 697-700 (1993). [PMID: 8489497]
  4. Mata, N. L., Tsin, A. T.
    Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes.
    Biochim. Biophys. Acta 1394 : 16-22 (1998). [PMID: 9767084]
  5. Ruiz, A., Winston, A., Lim, Y. H., Gilbert, B. A., Rando, R. R., Bok, D.
    Molecular and biochemical characterization of lecithin retinol acyltransferase.
    J. Biol. Chem. 274 : 3834-3841 (1999). [PMID: 9920938]

[EC created 1992, modified 2011]