Cytidine triphosphate: phosphatidic acid cytidyltransferase in Escherichia coli

Abstract

An enzyme has been found in particulate fractions of Escherichia coli that catalyzes the incorporation of cytidine triphosphate (CTP) into lipid in the presence of exogenous phosphatidic acid and Mg(++). The product has been identified enzymatically and by chromatography as cytidine diphosphate diglyceride. The reaction is optimal at a pH of 6.5 and Mg(++) concentration of 5-10 mm. The apparent K(m) for CTP is 7 x 10(-4)M and for phosphatidic acid, 2 x 10(-3)M. The reaction rate falls off rapidly with time and ceases entirely after 1 hr as the result of inactivation of the system by Mg(++).