Enzymatic characteristics of a Ser/Thr protein kinase, SpkA, from Myxococcus xanthus(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• Two Ser/Thr protein kinases, SpkA and SpkB, selected from Myxococcus xanthus based on amino acid sequence similarities with the catalytic subunits of cAMP-dependent protein kinases (PKA) were synthesized using a cell-free protein synthesis system. In various protein kinase assays, purified StkA and StkB showed their highest protein kinase activities in a PKA assay using the selective PKA substrate Kemptide and in a protein kinase C (PKC) assay using the selective PKC substrate neurogranin_<(28-43)>, respectively. SpkA had apparent K_m values of 45μM and 37μM for Kemptide and ATP, respectively. Phosphorylation of Kemptide was inhibited by a specific PKA inhibitor peptide, PKI_<5-24>, and the IC_<50> and K_i values for inhibition of the SpkA activity were 117nM and 36nM, respectively.

• 社団法人日本生物工学会の論文

著者

• TAKEGAWA Kaoru

  Department of Life Science, Faculty of Agriculture, Kagawa University

• Kakemizu Aoi

  Department Of Applied Biological Science Faculty Of Agriculture Kagawa University

• KIMURA YOSHIO

  Department of Life Science, Faculty of Agriculture, Kagawa University

• Takegawa Kaoru

  Department Of Applied Biological Science Faculty Of Agriculture Kagawa University:department Of Bios

• Matsubara Yuuko

  Department of Applied Biological Science, Faculty of Agriculture, Kagawa University

• Matsubara Yuuko

  Department Of Applied Biological Science Faculty Of Agriculture Kagawa University

• Kimura Yoshio

  Department Of Applied Biological Science Faculty Of Agriculture Kagawa University

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