CDP-diacylglycerol synthase activity in Clostridium perfingens

Journal Article · Fri Jan 01 00:00:00 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), Vol. 43:1
• Country of Publication: United States
• Language: English

Related Subjects

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