2.3.1.135 lecithin + 11-cis-retinol-[cellular retinol-binding protein] - 2.3.1.135 lecithin + all-trans-retinol-[cellular retinol-binding protein] - 2.3.1.135 lecithin + retinol-[cellular retinol-binding protein III] fatty acid retinyl esters are the storage form of vitamin A, all-trans-retinol, and serve as metabolic intermediates in the formation of the visual chromophore 11-cis-retinal, LRAT catalyzes the synthesis of retinyl esters, thereby drawing retinol from the circulation to storage depots 2.3.1.135 lecithin + retinol-[cellular retinol-binding protein III] the enzyme is responsible for catalyzing retinyl ester formation from retinol 2.3.1.135 lecithin + retinol-[cellular retinol-binding protein] - 2.3.1.135 additional information retinoids play an essential role in development and throughout life, levels in rat tissue after treatment with 2,3,7,8-tetrachlorodibenzo-4-dioxin, overview 2.3.1.135 additional information ARAT, EC 2.3.1.76, may complement LRAT to provide additional retinyl-ester synthase activity under conditions of high all-trans-retinol 2.3.1.135 additional information low prevalence of lecithin retinol acyltransferase mutations in patients with Leber congenital amaurosis and autosomal recessive retinitis pigmentosa 2.3.1.135 additional information LRAT is not required for retinoid isomerase activity beyond synthesis of retinyl-ester substrate, association of Rpe65 protein, a membrane-associated protein in the retinal pigment epithelium, with membranes is neither dependent upon LRAT nor the result of S-palmitoylation on Cys231, Cys329, and Cys330 by the enzyme, overview 2.3.1.135 additional information LRAT is required for retinoid storage and lipid droplet formation in hepatic stellate cells, LRAT is not the sole enzyme that catalyzes retinyl ester formation in vivo, role of LRAT in retinoid absorption and storage in different tissues, overview 2.3.1.135 additional information LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitamin A, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis 2.3.1.135 additional information LRAT plays an essential role in the regeneration of visual chromophore as well as in the metabolism of vitaminA, and is responsible for amidation of retinylamine, a potent and selective inhibitor of the retinoid cycle and 11-cis-retinal biosynthesis 2.3.1.135 additional information retinoids, vitamin A, i.e.retinol, and related metabolites, have been shown to be important in regulating cell growth and differentiation, retinoid signaling, overview, expression of LRAT, which converts retinol to retinyl esters, is reduced in several human carcinomas as compared with adjacent normal tissue from the same organs, LRAT protein progressively decreases with a reduction in the degree of tumor differentiation in invasive breast carcinomas, overview 2.3.1.135 additional information LRAT plays a role in maintaining a stable serum retinol concentration when dietary retinol concentration fluctuates 2.3.1.135 palmitoyl-CoA + 11-cis-retinol-[cellular retinol-binding protein] esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells 2.3.1.135 palmitoyl-CoA + all-trans-retinol-[cellular retinol-binding protein] esterification of 11-cis-retinol is four times greater than esterification of all-trans-retinol in Muller cells 2.3.1.135 phosphatidylcholine + 11-cis-retinol essential for generation of the precursor for 11-cis-retinal, the visual chromophore in the eye 2.3.1.135 phosphatidylcholine + 11-cis-retinol-[cellular-retinol-binding-protein] trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. 2.3.1.135 phosphatidylcholine + 11-cis-retinoll-[cellular-retinol-binding-protein] trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. 2.3.1.135 phosphatidylcholine + all-trans-retinol - 2.3.1.135 phosphatidylcholine + all-trans-retinol enzyme essential for the biosynthesis of 11-cis-retinal and for dietary mobilization of vitamin A 2.3.1.135 phosphatidylcholine + all-trans-retinol important role in absorption and storage of vitamin A 2.3.1.135 phosphatidylcholine + all-trans-retinol enzyme is involved in vitamin A storage and mobilization 2.3.1.135 phosphatidylcholine + all-trans-retinol LRAT catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to all-trans-retinol, vitamin A 2.3.1.135 phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] - 2.3.1.135 phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] enzyme and cellular retinol binding protein I, CRBP I are involved in retinoid storage regulation, retinoid biosynthetic pathway, overview 2.3.1.135 phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] enzyme is involved in the visual cycle in the eye 2.3.1.135 phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters and the retinoid cycle in the eye and in the liver 2.3.1.135 phosphatidylcholine + all-trans-retinol-[cellular-retinol-binding-protein] trans-esterification reaction is reversible, however in the presence of the isomerase, all-trans-retinyl esters are converted to 11-cis-retinol which is enzymatically oxidized to 11-cis-retinal, the chromophore of vision. Both all-trans-retinol and 11-cis-retinol are substrates for LRAT esterification, although all-transretinol is the preferred substrate. 2.3.1.135 phosphatidylcholine + all-trans-retinylamine - 2.3.1.135 phosphatidylcholine + retinol-[cellular-retinol-binding-protein] - 2.3.1.135 phosphatidylcholine + retinol-[cellular-retinol-binding-protein] renal cell carcinomata contain greatly reduced levels of retinol and retinyl esters relative to healthy kidney tissue 2.3.1.135 phosphatidylcholine + retinylamine -