InterPro domain: IPR027251

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 [ 1 , 2 , 3 , 4 , 5 ].

In mammals, DGAT1 is a multifunctional acyltransferase capable of synthesizing diacylglycerol, retinyl, and wax esters in addition to triacylglycerol [ 6 ]. In liver, it plays a role in esterifying exogenous fatty acids to glycerol [ 7 ]. 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 [ 8 ].

1. DGAT1 and PDAT1 acyltransferases have overlapping functions in Arabidopsis triacylglycerol biosynthesis and are essential for normal pollen and seed development. Plant Cell 21, 3885-901
2. The TAG1 locus of Arabidopsis encodes for a diacylglycerol acyltransferase. Plant Physiol. Biochem. 37, 831-840
3. Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase. Eur. J. Biochem. 267, 85-96
4. Arabidopsis mutants deficient in diacylglycerol acyltransferase display increased sensitivity to abscisic acid, sugars, and osmotic stress during germination and seedling development. Plant Physiol. 129, 1352-8
5. DGAT1, DGAT2 and PDAT expression in seeds and other tissues of epoxy and hydroxy fatty acid accumulating plants. Lipids 45, 145-57
6. A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J. Lipid Res. 46, 2388-97
7. The use of stable isotope-labeled glycerol and oleic acid to differentiate the hepatic functions of DGAT1 and -2. J. Lipid Res. 53, 1106-16
8. Retinol Esterification by DGAT1 Is Essential for Retinoid Homeostasis in Murine Skin. J. Biol. Chem. 284, 4292-9