Regulation of branched-chain α-ketoacid dehydrogenase kinase☆
References (50)
- et al.
Metabolism
(1982) - et al.
Advan. Enzyme Reg
(1977) - et al.
Biochim. Biophys. Acta
(1976) - et al.
J. Biol. Chem
(1982) - et al.
Biochem. Biophys. Res. Commun
(1982) - et al.
J. Biol. Chem
(1982) - et al.
Amer. J. Clin. Nutr
(1965) - et al.
J. Nutr
(1976) - et al.
J. Nutr
(1977) - et al.
FEBS Lett
(1972)
Biochem. Pharmacol
J. Biol. Chem
J. Biol. Chem
J. Biol. Chem
J. Biol. Chem
FEBS Lett
FEBS Lett
Arch. Biochem. Biophys
J. Biol. Chem
J. Biol. Chem
Arch. Biochem. Biophys
Metabolism
Biochem. Biophys. Res. Commun
J. Biol. Chem
J. Biol. Chem
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2023, Journal of Biological ChemistryEnergy metabolism profile of the effects of amino acid treatment on skeletal muscle cells: Leucine inhibits glycolysis of myotubes
2020, NutritionCitation Excerpt :The BCKDC is the rate-limiting enzyme for BCAA catabolism and regulated by inhibitory phosphorylation by BDK and activating dephosphorylation by mitochondrial phosphatase 2 C (PP2 Cm) [38,39]. Because BDK is also inhibited by KIC from leucine, resulting in the activation of BCKDC [40], the decreased glycolysis of myotubes by leucine might reflect the inhibition of BDK by KIC from leucine treatment. It has been reported that isoleucine, leucine, and its metabolite KIC promote glucose uptake in skeletal muscles of rats and cultured myotubes independent of mTOR signaling [41,42].
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2020, Rosenberg’s Molecular and Genetic Basis of Neurological and Psychiatric Disease: Volume 1Imbalanced dietary levels of branched-chain amino acids affect growth performance and amino acid utilization of juvenile red drum Sciaenops ocellatus
2018, AquacultureCitation Excerpt :Excess levels of dietary Leu are known to result in an imbalanced concentration of plasma BCAAs, where reduced levels of plasma Ile and Val have been found in humans (Matsumoto et al., 2014; Swendseid et al., 1965) and rats (Block and Harper, 1984; May et al., 1991). Authors have attributed this response to competitive inhibition during intestinal absorption and to the role of Leu as a promoter of the catabolism of BCAAs by activating BCKDH, the enzyme that catabolizes branched-chain α-keto acids (BCKAs) (Paxton and Harris, 1984). Similar results were found in rainbow trout by Yamamoto et al. (2004), reporting lower concentrations of Ile and Val in plasma when feeding diets formulated with an excess of Leu.
Ca<sup>2+</sup>-dependent inhibition of branched-chain α-ketoacid dehydrogenase kinase by thiamine pyrophosphate
2018, Biochemical and Biophysical Research Communications
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Supported in part by NIH Research Grants AM19259 and 5 S07 RR5371 and the Grace M. Showalter Residuary Trust.