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Biochemical characterization of Pkn2, a protein Ser/Thr kinase from Myxococcus xanthus , a Gram‐negative developmental bacterium
Author(s) -
Udo Hiroshi,
Inouye Masayori,
Inouye Sumiko
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01384-1
Subject(s) - myxococcus xanthus , autophosphorylation , staurosporine , biochemistry , protein kinase a , escherichia coli , kinase , biology , bacteria , glycerol kinase , microbiology and biotechnology , enzyme , gene , genetics , mutant
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 μM for ATP and 73 nmol/min/mg for V max . The optimum pH and temperature were determined to be 7.5 and 35°C, respectively. The autophosphorylation activity was inhibited by staurosporine with the IC 50 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.