Abstract
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.
Original language | English (US) |
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Pages (from-to) | 188-192 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 400 |
Issue number | 2 |
DOIs | |
State | Published - Jan 3 1997 |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Keywords
- Biochemical characterization
- Gram-negative bacteria
- Myxococcus xanthus
- Pkn2