Phosphatidylglycerophosphate synthase activity in Saccharomyces cerevisiae
- 1 October 1983
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 29 (10) , 1452-1457
- https://doi.org/10.1139/m83-222
Abstract
Cytidine 5′-diphospho-1,2-diacyl-sn-glycerol (CDP-diacylglycerol):sn-glycerol-3-phosphate phosphatidyltransferase (phosphatidylglycerophosphate synthase, EC 2.7.8.5) activity was characterized from the mitochondrial fraction of Saccharomyces cerevisiae. The pH optimum for the reaction was 7.0. Maximum activity was dependent on manganese (0.1 mM), magnesium (0.3 mM), or cobalt (1 mM) ions and the nonionic detergent Triton X-100 (1 mM). The apparent Km values for CDP-diacylglycerol and glycerol-3-phosphate were 33 and 27 μM, respectively. Optimal activity was at 30 °C with an energy of activation of 5.4 kcal/mol (1 cal = 4.1868 J). Phosphatidylglycerophosphate synthase activity was thermally labile above 40 °C. p-Chloromecuriphenylsulfonic acid, N-ethylmaleimide, and mercurous ions inhibited activity. Phosphatidylglycerophosphate synthase activity was partially solubilized from the mitochondrial fraction with 1% Triton X-100.This publication has 12 references indexed in Scilit:
- Phosphatidylglycerophosphate synthease and phosphatidylserine synthase activites in Clostridium perfringensJournal of Bacteriology, 1980
- Phosphatidylserine synthase from Escherichia coli. The role of Triton X-100 in catalysis.Journal of Biological Chemistry, 1979
- CTP-phosphatidic acid cytidyltransferase from Saccharomyces cerevisiae. Partial purification, characterization, and kinetic behaviorJournal of Biological Chemistry, 1978
- Purification and properties of phosphatidylgkycerophosphate synthetase from mammalian liver mitochondriaCanadian Journal of Biochemistry, 1978
- Intracellular Distribution of Enzymes of Phospholipid Metabolism in Several Gram-Negative BacteriaJournal of Bacteriology, 1977
- Membrane-associated phosphatidylglycerophosphate synthetase from Escherichia coli: purification by substrate affinity chromatography on cytidine 5'-diphospho-1,2-diacyl-sn-glycerol sepharoseBiochemistry, 1976
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Phosphatidylglycerol biosynthesis in Bacillus licheniformis. Resolution of membrane-bound enzymes by affinity chromatography on cytidinediphospho-sn-1,2-diacylglycerol sepharoseBiochemistry, 1976
- Phosphatidyl glycerophosphate phosphataseJournal of Lipid Research, 1967
- Biosynthesis of phosphatidyl glycerophosphate in Escherichia coliJournal of Lipid Research, 1967