Abstract
2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase is a membrane-bound enzyme that either activates fatty acids for acyl transfer in the presence of ATP and Mg 2+ or transfers fatty acids from acyl–acyl carrier protein (ACP) to the 1-position of lysophospholipids. 2-acyl-GPE acyltransferase is a heterodimer composed of a hydrophobic membrane-bound subunit and ACP. The catalytic cycle of the acyltransferase/synthetase is described in this chapter. The first step is the ligation of a fatty acid to the 4 ' -phosphopantetheine sulfhydryl group of the ACP subunit. The second step in the acyltransferase reaction is the transfer of the acyl moiety from ACP to the 2-acyl-GPE substrate to form phosphatidylethanolamine (PtdEtn). The assay method for 2-acyl-GPE acyltransferase is based on measuring the formation of [14C]PtdEtn from 2-acyl-GPE and [14C]palmitic acid in the presence of ATP, Mg 2+ , and ACP. A replica print procedure is used to isolate mutants lacking both 2-acyl-GPE acyltransferase and acyl-ACP synthetase activities. The acyltransferase/synthetase functions only as an acyltransferase in vivo ; its ability to synthesize acyl-ACP in vitro has made it a useful tool for the preparation of defined acyl-ACPs to be used as substrates for other enzymes.
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