LRAT-specific domain facilitates Vitamin A metabolism by domain swapping in HRASLS

LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3.

Cellular uptake of vitamin A, production of visual chromophore and triglyceride homeostasis in adipocytes depend on two representatives of the vertebrate N1pC/P60 protein family, lecithin:retinol acyltransferase (LRAT) and HRAS-like tumor suppressor 3 (HRASLS3). Both proteins function as lipid-metabolizing enzymes but differ in their substrate preferences and dominant catalytic activity. The me...

SUPPLEMENTARY INFORMATION LRAT-specific domain facilitates Vitamin A metabolism by domain swapping in HRASLS3

Membrane enzymes: transformers at the interface.

Membrane enzymes constitute a large class of proteins with vital roles in cellular signaling and metabolism and typically act on membrane components as substrates such as lipids or oligosaccharides of the bacterial cell wall1. The molecular basis of diverse reaction specificities of closely related membrane enzymes transforming identical substrates into different products has been largely elusi...

Topology and membrane association of lecithin: retinol acyltransferase.

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. Lecithin:retinol acyltransferase (LRAT), the main enzyme responsible for retinyl ester formation, acts by transferring an acyl group from the sn-1 position of phosphatidylcholine to retinol. To define the membrane associa...

Lecithin:retinol acyltransferase from mouse and rat liver. CDNA cloning and liver-specific regulation by dietary vitamin a and retinoic acid.

Lecithin:retinol acyltransferase (LRAT), present in microsomes, catalyzes the transfer of the sn-1 fatty acid of phosphatidylcholine to retinol bound to a cellular retinol-binding protein. In the present study we have cloned mouse and rat liver LRAT cDNA and tested the hypothesis that LRAT mRNA, like LRAT activity, is regulated physiologically in a liver-specific manner. The nucleotide sequence...