Inhibition of branched-chain alpha-ketoacid dehydrogenase kinase by thiamine pyrophosphate at different potassium ionic levels.
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.
Akita
Keiichi
K
Department of Materials Science and Engineering, Nagoya Institute of Technology, Nagoya, Japan.
Fujimura
Yukihiro
Y
Bajotto
Gustavo
G
Shimomura
Yoshiharu
Y
D000255:Adenosine Triphosphate / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D020128:Inhibitory Concentration 50; D007700:Kinetics; D011188:Potassium / Q000494:pharmacology*; D047428:Protein Kinase Inhibitors / Q000494:pharmacology*; D011494:Protein Kinases / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000494:pharmacology*
D047428:Protein Kinase Inhibitors; D000255:Adenosine Triphosphate; D011494:Protein Kinases; C035627:(3-methyl-2-oxobutanoate dehydrogenase (lipoamide)) kinase; D013835:Thiamine Pyrophosphate; D011188:Potassium