Biosynthesis of Cytidine Diphosphate-diglyceride by a Particulate Fraction from Micrococcus cerificans
Richard E. McCaman 1 and William R. Finnerty 1
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1 From the Institute of Psychiatric Research and Department of Microbiology, Indiana University School of Medicine, Indianapolis, Indiana 46207
The present study describes the isolation and partial purification of a particulate preparation from Micrococcus cerificans which actively catalyzes the net synthesis of CDP-diglyceride from CTP and phosphatidic acid. 14C-CTP was utilized to develop a sensitive quantitative assay for the phosphatidic acid cytidyltransferase.
A detailed study of the effects of various factors affecting the enzyme activity in vitro resulted in the observation that the bacterial enzyme has virtually an absolute requirement for K+ and a non-ionic detergent. These factors appear to represent the major differences between the bacterial and mammalian form of the enzyme. The specific activity of the best bacterial fraction thus far obtained (8000 µmoles per g of protein per hour) is nearly 100 times greater than any obtained thus far from mammalian sources. By utilizing the bacterial enzyme, it has been possible to produce CDP-diglyceride biosynthetically with a 58% efficiency based on phosphatidic acid utilization.
The primary role of CDP-diglyceride in the bacterial biosynthesis of essential phosphoglycerides as previously shown by other investigators now gains significant support by the demonstration of an active biosynthesis of this compound in bacterial extracts.
Submitted on April 4, 1968
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