Phospholipid:diacylglycerol acyltransferase (PDAT)

Phospholipid:diacylglycerol acyltransferase (PDAT) is an enzyme that catalyzes the acyl-CoA-independent synthesis of triacylglycerols (TAGs), which are the primary storage lipids in plants, yeast, and algae [1, 6, 21]. Unlike the classical Kennedy pathway that utilizes acyl-CoA, PDAT transfers a fatty acyl moiety from the sn-2 position of a phospholipid, such as phosphatidylcholine, to the sn-3 position of diacylglycerol (DAG) [2, 14, 61]. This reaction simultaneously produces TAG and a lysophospholipid, effectively linking the turnover of membrane lipids with the accumulation of storage lipids [36, 64]. While PDAT has been extensively characterized in agricultural biotechnology for its role in increasing seed oil content, recent evidence suggests the existence of human homologs, such as TMEM68, that perform similar functions in mammalian lipid metabolism [35, 54]. In the context of human health, PDAT is considered an emerging therapeutic target for metabolic diseases characterized by ectopic lipid accumulation, such as obesity and non-alcoholic fatty liver disease (NAFLD) [47, 49, 57]. By modulating PDAT activity, researchers aim to regulate the balance between membrane and storage lipids, potentially reducing the lipotoxic effects associated with excessive TAG and DAG levels [57]. Although no PDAT-targeted drugs are currently approved for clinical use, experimental small-molecule inhibitors are being developed and screened for their ability to treat metabolic disorders and for applications in industrial lipid production [40, 47].

Other names

Phospholipid:1,2-diacyl-sn-glycerol O-acyltransferasePDAT1LRO1Phosphatidylcholine:diacylglycerol acyltransferase

Acyl-CoA-independent transfer of a fatty acyl group from the sn-2 position of a phospholipid to the sn-3 position of diacylglycerol to form triacylglycerol.