TY - JOUR
T1 - Biochemical characterization of Pkn2, a protein Ser/Thr kinase from Myxococcus xanthus, a Gram-negative developmental bacterium
AU - Udo, Hiroshi
AU - Inouye, Masayori
AU - Inouye, Sumiko
N1 - Funding Information:
This work was supported by a grant from the National Institutes of Health (GM26843).
PY - 1997/1/3
Y1 - 1997/1/3
N2 - 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 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.
AB - 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 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.
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U2 - 10.1016/S0014-5793(96)01384-1
DO - 10.1016/S0014-5793(96)01384-1
M3 - Article
C2 - 9001395
AN - SCOPUS:0031015167
SN - 0014-5793
VL - 400
SP - 188
EP - 192
JO - FEBS Letters
JF - FEBS Letters
IS - 2
ER -