Diacylglycerol acyltransferase, reaction catalyzed

Acyl-CoA-independent processes have been identified that depend on either phosphatidylcholine (PC) or DAG as donors of fatty acyl moieties to DAG. These reactions are catalyzed by phospholipid diacylglycerol acyltransferase (PDAT) or diacylglycerol transacylase (DGTA), respectively. Complementary DNAs (cDNAs) encoding PDAT have been isolated (Dahlqvist et al. 2000, Stahl et al. 

Pan, X., Chen, G., Kazachkov, M., Greer, M.S., Caldo, K.M., Zou, J., Weselake, R.J., 2015. In vivo and in vitro evidence for biochemical coupling of reactions catalyzed by lysophosphatidyT choUne acyltransferase and diacylglycerol acyltransferase. J. Biol. Chem. 290, 18068-18078. 

This enzyme [EC 2.3.1.20], also known as diglyceride acyltransferase, catalyzes the reaction of an acyl-CoA with 1,2-diacylglycerol to produce coenzyme A and a triacylglycerol. The acyl-CoA derivative can be palmi-toyl-CoA or other long-chain acyl-CoA compounds. 

The pathways diverge at phosphatidate. In the synthesis of triacylglycerols, phosphatidate is hydrolyzed by a specific phosphatase to give a diacylglycerol (DAG). This intermediate is acylated to a triacylglycerol in a reaction that is catalyzed by diglyceride acyltransferase. Both enzymes are associated in a triacylglycerol synthetase complex that is bound to the endoplasmic reticulum membrane. 

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