HOSPHATIDYLGLYCEROPHOSPHATE SYNTHASE FROM GERMINATING SOYBEANS

George Carman, ANDREW S. GREENBERG

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)321-333
Number of pages13
JournalJournal of Food Biochemistry
Volume8
Issue number4
DOIs
StatePublished - Jan 1 1984

All Science Journal Classification (ASJC) codes

  • Food Science
  • Biophysics
  • Pharmacology
  • Cell Biology

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