Molecular and biochemical characterization of lecithin retinol acyltransferase.

Article Details

Citation

Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D

Molecular and biochemical characterization of lecithin retinol acyltransferase.

J Biol Chem. 1999 Feb 5;274(6):3834-41.

PubMed ID
9920938 [ View in PubMed
]
Abstract

The enzyme responsible for conversion of all-trans-retinol into retinyl esters, the lecithin retinol acyltransferase (LRAT) has been characterized at the molecular level. The cDNA coding for this protein was cloned and its amino acid sequence deduced. LRAT is composed of a polypeptide of 230 amino acid residues with a calculated mass of 25.3 kDa. Tissue distribution analysis by Northern blot showed expression of a 5.0-kilobase transcript in the human retinal pigment epithelium as well as in other tissues that are known for their high LRAT activity and vitamin A processing. Affinity labeling experiments using specific compounds with high affinity for LRAT and monospecific polyclonal antibodies raised in rabbits against two peptide sequences for LRAT confirmed the molecular mass of LRAT as a 25-kDa protein. High performance liquid chromatography analysis of the reaction product formed by HEK-293 cells transfected with LRAT cDNA confirmed the ability of the transfected cells to convert [3H]all-trans-retinol into authentic [3H]all-trans-retinyl palmitate as chemically determined.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Lecithin retinol acyltransferaseO95237Details