@article{oai:nagoya.repo.nii.ac.jp:00027071, author = {Noguchi, Seisuke and Kondo, Yusuke and Ito, Rina and Katayama, Takahiro and Kazama, Shunsuke and Kadota, Yoshihiro and Kitaura, Yasuyuki and Harris, Robert A. and Shimomura, Yoshiharu}, issue = {4}, journal = {Biochemical and Biophysical Research Communications}, month = {Oct}, note = {Catabolism of the branched-chain amino acids (BCAAs: leucine, isoleucine, and valine) is regulated by the branched-chain α-ketoacid dehydrogenase (BCKDH) complex, which in turn is regulated by phosphorylation catalyzed by BCKDH kinase (BDK). Thiamine pyrophosphate (TPP) is required as a coenzyme for the E1 component of the BCKDH complex and can also bring about activation of the complex by inhibiting BDK. The present study shows that free Ca^2+ in the physiological range greatly increases the sensitivity of BDK to inhibition by TPP (IC50 of 2.5 μM in the presence of 1 μM free Ca^2+). This novel mechanism may be responsible for the stimulation of BCAA oxidation by conditions that increase mitochondrial free Ca^2+ levels, e.g. in skeletal muscle during exercise., ファイル公開:2019-10-12}, pages = {916--920}, title = {Ca2+-dependent inhibition of branched-chain α-ketoacid dehydrogenase kinase by thiamine pyrophosphate}, volume = {504}, year = {2018} }