HOSPHATIDYLGLYCEROPHOSPHATE SYNTHASE FROM GERMINATING SOYBEANS1

Phosphatidylglycerophosphate synthase (CDP-diacylglycerol: sn-glycerol-3-phosphate phosphatidyltransferase, EC 2.7.8.5) activity was identified from the crude mitochondrial fraction of germinating soybeans. The mitochondrial enzyme exhibited pH optima at 7.0 and 9.5. Phosphatidylglycerophosphate was the predominate product at pH 9.5 while phosphatidylglycerol was the predominate product at pH 7.0. At pH 9.5, maximum phosphatidylglycerophosp-hate synthase activity was dependent on manganese (0.5 mM), magnesium (10 mM), or cobalt (20 mM) ions and Triton X-100 (0.5 mM). The apparent Km values for CDP-diacylglycerol and glycerol-3-phos-phate were 0.1 mM and 0.17 mM, respectively. Activity was completely stable to temperatures up to 70°C and the energy of activation was 3.16 Kcallmole. Thioreactive agents slightly inhibited activity.

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