Carter J R
J Lipid Res. 1968 Nov;9(6):748-54.
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(++).
在大肠杆菌的颗粒组分中发现了一种酶，该酶在外源磷脂酸和Mg(++)存在的情况下，催化三磷酸胞苷（CTP）掺入脂质中。该产物已通过酶法和色谱法鉴定为二磷酸胞苷二甘油酯。该反应在pH 6.5和Mg(++)浓度为5 - 10 mM时最适宜。CTP的表观K(m)为7×10(-4)M，磷脂酸的表观K(m)为2×10(-3)M。反应速率随时间迅速下降，1小时后由于系统被Mg(++)灭活而完全停止。
