Biosynthesis of phosphatidyl glycerophosphate in Escherichia coli

作者：Ying-Ying Chang, Eugene Paul Kennedy · 发表于：Journal of Lipid Research · 年份：1967 · DOI：10.1016/s0022-2275(20)38901-x · 被引用次数：223 · 研究领域：Lipid metabolism and biosynthesis、Enzyme Catalysis and Immobilization、Microbial Metabolic Engineering and Bioproduction

An enzyme (L-glycerol 3-phosphate: CMP phosphatidyltransferase) catalyzing the synthesis of phosphatidyl glycerophosphate from CDP-diglyceride and L-glycerol 3-phosphate has been rendered soluble by treatment of the particulate, membrane-containing fraction of E. coli with Triton X-100 and has been partially purified. The enzyme, devoid of phosphatidyl glycerophosphatase activity, is specific for L-glycerol 3-phosphate and is completely dependent upon added Mg(++) or Mn(++) for activity. It has high affinity for CDP-diglyceride and can be used for the assay of this nucleotide. Other properties of the enzyme are also described.