TY - JOUR
T1 - Enzymatic characteristics of a Ser/Thr protein kinase, SpkA, from Myxococcus xanthus
AU - Kimura, Yoshio
AU - Kakemizu, Aoi
AU - Matsubara, Yuuko
AU - Takegawa, Kaoru
N1 - Funding Information:
This study was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (18570131).
PY - 2009/1
Y1 - 2009/1
N2 - 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 Km values of 45 μM and 37 μM for Kemptide and ATP, respectively. Phosphorylation of Kemptide was inhibited by a specific PKA inhibitor peptide, PKI5-24, and the IC50 and Ki values for inhibition of the SpkA activity were 117 nM and 36 nM, respectively.
AB - 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 Km values of 45 μM and 37 μM for Kemptide and ATP, respectively. Phosphorylation of Kemptide was inhibited by a specific PKA inhibitor peptide, PKI5-24, and the IC50 and Ki values for inhibition of the SpkA activity were 117 nM and 36 nM, respectively.
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U2 - 10.1016/j.jbiosc.2008.08.002
DO - 10.1016/j.jbiosc.2008.08.002
M3 - Article
C2 - 19147102
AN - SCOPUS:58149291455
SN - 1389-1723
VL - 107
SP - 10
EP - 15
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 1
ER -