| http://purl.uniprot.org/citations/2822695 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2822695 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2822695 | http://www.w3.org/2000/01/rdf-schema#comment | "The membrane-associated phospholipid biosynthetic enzyme CDP-diacylglycerol synthase (CTP:phosphatidate cytidylyltransferase, EC 2.7.7.41) was purified 2,300-fold from Saccharomyces cerevisiae. The purification procedure included Triton X-100 solubilization of mitochondrial membranes, CDP-diacylglycerol-Sepharose affinity chromatography, and hydroxylapatite chromatography. The procedure resulted in a nearly homogeneous enzyme preparation as determined by native and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Radiation inactivation of mitochondrial associated and purified CDP-diacylglycerol synthase suggested that the molecular weight of the native enzyme was 114,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme preparation yielded two subunits with molecular weights of 56,000 and 54,000. Antibodies prepared against the purified enzyme immunoprecipitated CDP-diacylglycerol synthase activity and subunits. CDP-diacylglycerol synthase activity was dependent on magnesium ions and Triton X-100 at pH 6.5. Thio-reactive agents inhibited activity. The activation energy for the reaction was 9 kcal/mol, and the enzyme was thermally labile above 30 degrees C. The Km values for CTP and phosphatidate were 1 and 0.5 mM, respectively, and the Vmax was 4,700 nmol/min/mg. Results of kinetic and isotopic exchange reactions suggested that the enzyme catalyzes a sequential Bi Bi reaction mechanism."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)47833-7"xsd:string |
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| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/author | "Kelley M.J."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/author | "Kelley M.J."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/pages | "14563-14570"xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/pages | "14563-14570"xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/title | "Purification and characterization of CDP-diacylglycerol synthase from Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/title | "Purification and characterization of CDP-diacylglycerol synthase from Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/volume | "262"xsd:string |
| http://purl.uniprot.org/citations/2822695 | http://purl.uniprot.org/core/volume | "262"xsd:string |
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| http://purl.uniprot.org/citations/2822695 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2822695 |
| http://purl.uniprot.org/uniprot/P38221 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2822695 |
| http://purl.uniprot.org/uniprot/P38221#attribution-E3C6CF7F89E41960FC58174C32C495AB | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/2822695 |