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Enzymatic characteristics of a Ser/Thr protein kinase, SpkA, from Myxococcus xanthus

Paper ID Volume ID Publish Year Pages File Format Full-Text
21947 43245 2009 6 PDF Available
Title
Enzymatic characteristics of a Ser/Thr protein kinase, SpkA, from Myxococcus xanthus
Abstract

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.

Keywords
Myxococcus xanthus; Ser/Thr protein kinase; Bacteria; PKA; Kemptide; PKI inhibitor
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 107, Issue 1, January 2009, Pages 10–15
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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Full-text PDF Download
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Any Questions? feel free to contact us