Abstract
Cytidine diphosphate-diacylglycerol (CDP-DG) synthase activity (EC 2.7.7.41) of a microsomal membrane preparation from suspension cultured Catharanthus roseus cells was characterized. The enzyme showed a pH optimum of 7.3 and apparent K m values for cytidine triphosphate (CTP) and phosphatidic acid (PA) of 170 and 80 μM, respectively. Inhibition was observed with CDP and inorganic pyrophosphate (PPi) with apparent K i values of 240 μM and about 1.5 mM, respectively. After extraction from the microsomal membranes, the enzyme was further purified with Phenyl-Sepharose chromatography, although the yield was low. CDP-DG synthase is obviously a membrane-bound protein and located both in intracellular membranes, i.e. the endoplasmic reticulum (ER), the mitochondrial and chloroplast envelopes and the plasma membrane.
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