Open AccessFunctional characteristics of phosphatidylinositol‐specific phospholipases C from Bacillus cereus and Bacillus thuringiensis
Author(s) -
Volwerk Johannes J.,
Koke John A.,
Wetherwax Peter B.,
Griffith O.Hayes
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03629.x
Subject(s) - bacillus thuringiensis , bacillus cereus , phospholipase c , phosphatidylinositol , biochemistry , cereus , bacillales , phospholipase , biology , hydrolysis , bacillaceae , enzyme , bacteria , bacillus subtilis , signal transduction , genetics
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.