Open AccessPurification and characterization of an ATP‐dependent protein kinase from Streptococcus faecalis
Author(s) -
Deutscher J.,
Engelmann R.
Publication year - 1984
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.1574-6968.1984.tb01053.x
Subject(s) - enterococcus faecalis , biochemistry , pep group translocation , streptococcus pyogenes , bacillus subtilis , streptococcus , kinase , enzyme , phosphotransferase , fructose , biology , protein kinase a , microbiology and biotechnology , phosphofructokinase 2 , escherichia coli , chemistry , bacteria , staphylococcus aureus , phosphoenolpyruvate carboxykinase , genetics , gene
An enzyme catalyzing the ATP‐dependent phosphorylation of HPr of the bacterial phosphotransferase system has been purified from Streptococcus faecalis . Size exclusion chromatography and sodium dodecyl sulfate (SDS) polyacrylamide gels revealed an M r of 65000. Beside HPr of S. faecalis the protein kinase also phosphorylates HPr of Streptococcus lactis, Streptococcus pyogenes, Bacillus subtilis and Streptococcus aureus , but not HPr of Escherichia coli . The kinase is largely inhibited by P i and EDTA. Mg 2+ and Mn 2+ could overcome inhibition by EDTA. 2‐Phosphoglycerate and glucose‐6‐phosphate, previously reported to stimulate kinase activity in crude extracts, had no effect on the purified enzyme. Fructose‐1,6‐diphosphate stimulated the protein kinase.