The MBOAT (membrane bound O-acyl transferase) family of membrane proteins contains a variety of acyltransferase enzymes. A conserved histidine has been suggested to be the active site residue []. The structure of MBOAT has been revealed [].This family includes Diacylglycerol O-acyltransferase 1 (DGAT1) and Lysophospholipid acyltransferase 7 (MBOAT7) from humans. DGAT1 catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates []. It also functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders []. MBOAT7 participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation [].
Diacylglycerol O-acyltransferase 1 (DGAT1) catalyses the final step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In plants, diacylglycerol O-acyltransferase 1 (DGAT1, TAG1) is a major enzyme for oil accumulation in seeds. It has complementary functions with PDAT1 acyltransferase that are essential for triacylglycerol synthesis and normal development of both seeds and pollen [, , , , ].In mammals, DGAT1 is a multifunctional acyltransferase capable of synthesizing diacylglycerol, retinyl, and wax esters in addition to triacylglycerol []. In liver, it plays a role in esterifying exogenous fatty acids to glycerol []. It also functions as the major acyl-CoA retinol acyltransferase in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders [].
