Properties of two sugar phosphate phosphatases from Streptococcus bovis and their potential involvement in inducer expulsion.
Streptococcus bovis possesses two sugar phosphate phosphatases (Pases). Pase I is a soluble enzyme that is inhibited by the membrane fractions from lactose-grown cells and is insensitive to activation by S46D HPr, an analog of HPr(ser-P) of the sugar phosphotransferase system. Pase II is a membrane-associated enzyme that can be activated 10-fold by S46D HPr, and it appears to play a role in inducer expulsion.
Cook
G M
GM
Section of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Ye
J J
JJ
Russell
J B
JB
Saier
M H
MH
D001426:Bacterial Proteins; D002458:Cell Fractionation; D004789:Enzyme Activation; D008756:Methylgalactosides / Q000378:metabolism*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D016985:Streptococcus bovis / Q000201:enzymology* / Q000378:metabolism; D013403:Sugar Phosphates / Q000378:metabolism*; D013862:Thiogalactosides / Q000378:metabolism*
D001426:Bacterial Proteins; D008756:Methylgalactosides; D013403:Sugar Phosphates; D013862:Thiogalactosides; C009468:thiomethylgalactoside; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; D010744:Phosphoric Monoester Hydrolases