Biochemical characterization of Pkn2, a protein Ser/Thr kinase from Myxococcus xanthus, a gram-negative developmental bacterium

被引：18
|
作者：
Udo, H [1 ]
Inouye, M [1 ]
Inouye, S [1 ]
机构：
[1] UNIV MED & DENT NEW JERSEY, ROBERT WOOD JOHNSON MED SCH, DEPT BIOCHEM, PISCATAWAY, NJ 08854 USA
来源：
FEBS LETTERS | 1997年 / 400卷 / 02期
关键词：
Pkn2; biochemical characterization; gram-negative bacteria; Myxococcus xanthus;
D O I：
10.1016/S0014-5793(96)01384-1
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 K-m value of 177 mu M for ATP and 73 nmol/min/mg for V-max. 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.
引用
收藏
页码：188 / 192
页数：5
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