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

页码：188 / 192

页数：5