CDP-diacylglycerol synthase activity in Clostridium perfringens

G. M. Carman, R. L. Zaniewski, J. J. Cousminer

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

CTP:phosphatidate cytidylyltransferase (CDP-diacylglycerol synthase; EC 2.7.7.41) was identified in the cell envelope fraction of the gram-positive anaerobe C. perfringens. The association of this enzyme with the cell envelope fraction of cell extracts was demonstrated by glycerol density gradient centrifugation and by activity sedimenting with the 100,000 x g pellet. The enzyme exhibited a broad pH optimum between pH 6.5 and pH 7.5. Enzyme activity was dependent on magnesium (5 mM) or manganese (1mM) ions. Activity was also dependent on the addition of the nonionic detergent Triton X-100 (5 mM). The apparent K(m) values for CTP and phosphatidic acid were 0.18 mM and 0.22 mM, respectively. Thioreactive agents inhibited activity, indicating that a sulfhydryl group is essential for activity. Maximal enzyme activity was observed at 50°C.

Original languageEnglish (US)
Pages (from-to)81-85
Number of pages5
JournalApplied and environmental microbiology
Volume43
Issue number1
StatePublished - Jan 1 1982

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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