CDP-diacylglycerol synthase activity in Clostridium perfingens

Journal Article · Fri Jan 01 04:00:00 EST 1982 · Appl. Environ. Microbiol.; (United States)

OSTI ID:5036657

Carmen, G M; Zaniewski, R L; Cousminer, J J

CTP: phosphatidate cytidylyltransferase (CDP-diacylglycerol synthase; EC 2.7.7.41) was identified in the cell envelope fraction of the gram-positive anaerobe Clostridium 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 optimium between pH 6.5 and pH 7.5. Enzyme activity was dependent on magnesium (5 mM) or manganese (1 mM) ions. Activity was also dependent on the addition on the nonionic detergent Triton X-100 (5 mM). The apparent Km 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 degrees C. (Refs. 24).

• Research Organization: Dept of Food Science, Cook Coll, New Jersey, Agricultural Experiment Station, Rutgers Univ, New Brunswick, New Jersey 08903
• OSTI ID: 5036657
• Journal Information: Appl. Environ. Microbiol.; (United States), Journal Name: Appl. Environ. Microbiol.; (United States) Vol. 43:1; ISSN AEMID
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
ALCOHOLS
BACTERIA
CENTRIFUGATION
CLOSTRIDIUM
ELEMENTS
ENZYME ACTIVITY
ENZYMES
GLYCEROL
HYDROXY COMPOUNDS
MANGANESE
MEMBRANES
METALS
MICROORGANISMS
ORGANIC COMPOUNDS
PH VALUE
PROTEINS
SEPARATION PROCESSES
TEMPERATURE EFFECTS
TRANSFERASES
TRANSITION ELEMENTS