Phosvitin kinase activity in Acholeplasma axanthum.
Incubating the soluble fraction derived from A. axanthum with phosvitin and [gamma-32P]ATP results in the phosphorylation of phosvitin. Casein, histone and kemptide were practically ineffective substrates, whereas a 55 kDa protein of M. gallisepticum was efficiently phosphorylated. The enzymatic activity has an optimal pH in the pH range 6.0-6.2 and requires divalent cations. The activity was inhibited by ammonium sulfate, heparin and sulphydryl blocking reagents, but was not affected by calmodulin with or without Ca2+ or by cyclic AMP.
Platt
M W
MW
Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Rottem
S
S
D000127:Acholeplasma / Q000201:enzymology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D002413:Cations, Divalent; D006863:Hydrogen-Ion Concentration; D009174:Mycoplasma; D010766:Phosphorylation; D010774:Phosvitin / Q000378:metabolism; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D012969:Sodium Fluoride / Q000494:pharmacology; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D001426:Bacterial Proteins; D002413:Cations, Divalent; D047428:Protein Kinase Inhibitors; D000644:Quaternary Ammonium Compounds; D013439:Sulfhydryl Reagents; D000255:Adenosine Triphosphate; D012969:Sodium Fluoride; D010774:Phosvitin; D011494:Protein Kinases