2-Acylglycerolphosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase is a membrane-associated acyl carrier protein binding protein.

摘要: Abstract Two enzymatic activities, 2-acylglycerolphosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase, were solubilized purified from Escherichia coli membranes. Electrophoretic analysis of the final product purification procedure revealed a single species with an apparent molecular mass 27 kilodaltons. The ratio to synthetase activities remained same throughout scheme indicating that both catalyzed by enzyme. 2-Acyl-GPE exhibited ACP Km 64 nM under standard assay conditions increased 10 microM when was conducted in presence 0.4 M LiCl. Acyl-ACP activity not detected absence LiCl, for this reaction 16 microM. Direct evidence subunit acyltransferase/synthetase obtained adsorption catalytic ACP-Sepharose affinity column binding [3H]ACP enzyme preparation. acyl-ACP 13 microM, rate acyl transfer donor enhanced addition LiCl exchange enzyme-bound determinant factor phosphatidylethanolamine formation acyl-ACP. These data indicate 2-acyl-GPE reactions are membrane possesses high site soluble ACP.