Biosynthesis of phosphatidyl glycerophosphate in Escherichia coli.
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.
D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000201:enzymology*; D005989:Glycerides; D005994:Glycerophosphates / Q000096:biosynthesis; D007477:Ions; D008274:Magnesium; D008345:Manganese; D010743:Phospholipids / Q000096:biosynthesis; D013501:Surface-Active Agents; D014166:Transferases / Q000032:analysis*
D005989:Glycerides; D005994:Glycerophosphates; D007477:Ions; D010743:Phospholipids; D013501:Surface-Active Agents; D008345:Manganese; D014166:Transferases; D008274:Magnesium