Biochemical characterization of Pkn2, a protein Ser/Thr kinase from Myxococcus xanthus, a Gram-negative developmental bacterium.
Pkn2, a protein Ser/Thr kinase, from the developmental bacterium Myxococcus xanthus was expressed under a T7 promoter in Escherichia coli and purified. Purified Pkn2 retained the autophosphorylation activity with the Km value of 177 microM for ATP and 73 nmol/min/mg for Vmax. The optimum pH and temperature were determined to be 7.5 and 35 degrees C, respectively. The autophosphorylation activity was inhibited by staurosporine with the IC50 value of 400 nM while H-7 and genistein had little effect on this kinase. Pkn2 appears to be unique for its higher manganese dependence. This is the first biochemical characterization of the prokaryotic protein Ser/Thr kinase.
Udo
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Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
Inouye
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M
Inouye
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D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism; D007477:Ions; D008274:Magnesium; D008345:Manganese; D008670:Metals; D016941:Myxococcus xanthus / Q000201:enzymology*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D007477:Ions; D008670:Metals; D008345:Manganese; C093969:Pkn2 kinase; D017346:Protein Serine-Threonine Kinases; D008274:Magnesium