Functional characteristics of phosphatidylinositol-specific phospholipases C from Bacillus cereus and Bacillus thuringiensis.
Phosphatidylinositol-specific phospholipase C was purified from the culture medium of B. thuringiensis to high specific activity using a procedure we recently described for purification of PI-PLC from B. cereus (Volwerk et al. (1989) J. Cell. Biochem. 39, 315-325). The purified enzymes from B. thuringiensis and B. cereus have similar specific activities towards hydrolysis of the membrane lipid phosphatidylinositol, and also towards hydrolysis of the glycosyl-phosphatidylinositol-containing membrane anchor of bovine erythrocyte acetylcholinesterase. These results indicate very similar catalytic properties for the structurally homologous PI-specific phospholipases C secreted by these bacilli.
Volwerk
J J
JJ
Institute of Molecular Biology, University of Oregon, Eugene.
Koke
J A
JA
Wetherwax
P B
PB
Griffith
O H
OH
D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D001407:Bacillus / Q000378:metabolism*; D001409:Bacillus cereus / Q000378:metabolism; D001413:Bacillus thuringiensis / Q000378:metabolism; D002417:Cattle; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology; D006868:Hydrolysis; D066298:In Vitro Techniques; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000378:metabolism*; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism* / Q000494:pharmacology
D010716:Phosphatidylinositols; D000110:Acetylcholinesterase; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase