Lysophosphatidylcholine acyltransferase LPCAT

DAG produced via the action of PA phosphatase can also be converted to PC by the catalytic action of choline phosphotransferase (CPT). Production of polyunsaturated FAs via the catalytic action of membrane-bound desaturases occurs while monounsaturated FAs are esterifled to the glycerol backbone of PC. The combined forward and reverse reactions catalyzed by lysophosphatidylcholine acyltransferase (LPCAT) are believed to facilitate acyl exchange at the sn-2 position of PC, with the acyl-CoA pool thereby allowing incorporation of polyunsaturated FA into TAG via the acyl-CoA-dependent acyltransferase reactions in the mainstream of TAG biosynthesis. The reverse reaction of CPT to produce DAG provides a second opportunity to introduce polyunsaturated FA into TAG. In addition, phospholipase A2 may catalyze the release of free FA from PC. The liberated FA could be reesterified as acyl-CoA for use in the mainstream of TAG biosynthesis. 

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