EC Number |
General Information |
Reference |
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2.3.1.135 | evolution |
based on its secondary structure LRAT belongs to a superfamily of enzymes generically referred as NIpC/P60. Within this superfamily, a multiple sequence alignment of LRAT and LRAT-like family members shows that they share three conserved amino acid residues; cysteine, histidine and a polar residue that is thought to complete a catalytic triad similar to the papain-like thiol peptidases |
719417 |
2.3.1.135 | malfunction |
a truncated form of LRAT as well as its S175R mutant lead to retinis pigmentosa, a severe form of retinal dystrophy |
719418 |
2.3.1.135 | malfunction |
generation of an animal model in which the lrat gene is disrupted by homologous recombination gives Lrat-/- mice, which show slow degeneration of their retinas, essentially a shortening of rod outer segments and highly attenuated electroretinograms |
719417 |
2.3.1.135 | malfunction |
homozygous mutation S175R occurs in two patients diagnosed with severe early-onset retinal degeneration |
719417 |
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 |
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 | 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 | more |
the catalytic triad includes histidine 60, tyrosine 154 and cysteine 161 in the LRAT structure |
719418 |
2.3.1.135 | physiological function |
activities of LRAT and RPE65 may be important for removal of all-trans retinal which is the substrate for retinoic acid production in skin cells. Decreasing cellular amount of retinoic acid and its precursor molecules might result in a change of gene regulation |
715720 |
2.3.1.135 | physiological function |
cellular retinol-binding protein CRBP I effectively conveys retinol to the LRAT, thereby circumventing the low enzymatic activity of LRAT in polar bear livers |
758200 |