Document Detail

Inhibition of branched-chain alpha-ketoacid dehydrogenase kinase by thiamine pyrophosphate at different potassium ionic levels.
MedLine Citation:
PMID:  19420697     Owner:  NLM     Status:  MEDLINE    
Inhibition of branched-chain alpha-ketoacid dehydrogenase kinase (BDK) by thiamine pyrophosphate (TPP) was analyzed at two potassium ion (K(+)) concentrations. IC(50) values of 4.6 and 8.0 microM and inhibition constant values of 3.2 and 16.4 microM were obtained in the presence of 20 and 100 mM K(+), respectively. These results suggest that BDK is less sensitive to TPP inhibition under physiological TPP and K(+) concentrations.
Keiichi Akita; Yukihiro Fujimura; Gustavo Bajotto; Yoshiharu Shimomura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-05-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  73     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-05-25     Completed Date:  2009-08-28     Revised Date:  2012-06-06    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1189-91     Citation Subset:  IM    
Department of Materials Science and Engineering, Nagoya Institute of Technology, Nagoya, Japan.
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MeSH Terms
Adenosine Triphosphate / pharmacology
Dose-Response Relationship, Drug
Inhibitory Concentration 50
Potassium / pharmacology*
Protein Kinase Inhibitors / pharmacology*
Protein Kinases / metabolism*
Thiamine Pyrophosphate / pharmacology*
Reg. No./Substance:
0/Protein Kinase Inhibitors; 154-87-0/Thiamine Pyrophosphate; 56-65-5/Adenosine Triphosphate; 7440-09-7/Potassium; EC 2.7.-/Protein Kinases; EC dehydrogenase (lipoamide)) kinase

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