EC Number |
General Information |
Reference |
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2.3.1.135 | more |
malignant melanoma cells are able to esterify all-trans retinol and subsequently isomerize all-trans retinyl esters into 11-cis retinol, whereas their benign counterpart melanocytes are not able to catalyze these reactions |
715720 |
2.3.1.135 | physiological function |
quiescent LRAT knockout hepatic stellate cells retain the capacity to synthesize retinyl esters and to store neutral lipids in lipid droplets ex vivo. The median lipid droplet size in LRAT knockout hepatic stellate cells (1080 nm) is significantly smaller than in wild-type stellate cells (1618 nm). Upon prolonged (24h) incubation, the amounts of small (less than 700 nm) lipid droplets strongly increases both in wild type and in LRAT knockout hepatic stellate cells |
756085 |
2.3.1.135 | physiological function |
relationship between LRAT and Crbp1 during retinyl ester biosynthesis in which mitochondria associated membranes-associated Crpb1 and LRAT colocalize, and both surround the growing retinyl ester-containing lipid droplet. The N-terminus of LRAT, especially K36 and R38, is essential to colocalization with the lipid droplet |
718992 |
2.3.1.135 | physiological function |
retinoid isomerohydrolase RPE65 palmitoylation level is highly regulated by lecithin:retinol acyltransferase (LRAT) enzyme. In the presence of LRAT substrate all-trans retinol, there is a significant decrease in the level of palmitoylation of RPE65 |
758452 |
2.3.1.135 | more |
the catalytic triad includes histidine 60, tyrosine 154 and cysteine 161 in the LRAT structure |
719418 |
2.3.1.135 | metabolism |
the key step of vitamin A metabolism is the esterification of all-trans retinol, catalyzed by lecithin/retinol acyltransferase, LRAT. Vitamin A metabolism in benign and malignant melanocytic skin cells with regard to expression, functional activity of LRAT, RPE65, and cRBP2 and their regulation, overview |
715720 |
2.3.1.135 | malfunction |
vitamin A uptake from recombinant holo-retinol-binding protein exhibited by wild-type mice is impaired in Lrat-deficient mice. Lrat-/- mice show elevated cellular vitamin A-binding protein 1, CRBP1, protein in the liver, lung, and adipose tissue as compared with wild type control animals |
-, 720030 |