Open AccessProtein kinase activities in cell‐free extracts of Rhodomicrobium vannielii
Author(s) -
Turner Andrew M.,
Mann Nicholas H.
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.tb03353.x
Subject(s) - kinase , biochemistry , phosphatase , protein kinase a , calmodulin , phosphorylation , enzyme , chemistry , biology
Using dialysed cell‐free extracts of the purple non‐sulphur bacterium Rhodomicrobium vannielii protein kinase activities capable of transferring the gamma phosphate group from gamma [ 32 P]ATP to a variety of polypeptides were detected. The optimum concentration of Mg 2+ for protein kinase activity was about 20 mM and the phosphorylation of one polypeptide ( M r 47 kDa) was inhibited by chlorpromazine, a calmodulin antagonist, and also by Ca 2+ . The activity of at least one of the protein kinases (or a phosphatase) was regulated by ribulose 1,5‐bisphosphate.