Regulation of branched-chain amino acid catabolism: Nutritional and hormonal regulation of activity and expression of the branched-chain α-keto acid dehydrogenase kinase

Yoshiharu Shimomura, Mariko Obayashi, Taro Murakami, Robert Harris

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

Branched-chain α-keto acid dehydrogenase kinase is responsible for the inactivation and phosphorylation of the branched-chain α-keto acid dehydrogenase complex, the enzyme that catalyses the committed step of branched-chain amino acid catabolism. The activity of the branched-chain α-keto acid dehydrogenase complex is inversely correlated with kinase activity, suggesting that the relative activity of the kinase is the primary regulator of the activity of the complex. It has been shown that kinase activity and expression are affected by nutritional states imposed by low-protein diet feeding, starvation, diabetes, and exercise. Evidence has also been presented that certain hormones, particularly insulin, glucocorticoid, thyroid hormone and female sex hormones, affect the activity and expression of the kinase. The findings indicate that nutritional and hormonal control of the activity and expression of branched-chain α-keto acid dehydrogenase kinase provides an important means of control of the activity of the branched-chain α-keto acid dehydrogenase complex, with inactivation serving to conserve branched-chain amino acids for protein synthesis in some situations and activation serving to provide carbon for gluconeogenesis in others.

Original languageEnglish (US)
Pages (from-to)419-423
Number of pages5
JournalCurrent Opinion in Clinical Nutrition and Metabolic Care
Volume4
Issue number5
DOIs
StatePublished - 2001
Externally publishedYes

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3-methyl-2-oxobutanoate dehydrogenase (lipoamide)
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Branched Chain Amino Acids
branched chain amino acids
amino acid metabolism
hormonal regulation
phosphotransferases (kinases)
Phosphotransferases
inactivation
Protein-Restricted Diet
Gluconeogenesis
gluconeogenesis
sex hormones
low protein diet
Gonadal Steroid Hormones
thyroid hormones
glucocorticoids
Starvation
Thyroid Hormones
Glucocorticoids

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Endocrinology
  • Food Science
  • Endocrinology, Diabetes and Metabolism

Cite this

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T2 - Nutritional and hormonal regulation of activity and expression of the branched-chain α-keto acid dehydrogenase kinase

AU - Shimomura, Yoshiharu

AU - Obayashi, Mariko

AU - Murakami, Taro

AU - Harris, Robert

PY - 2001

Y1 - 2001

N2 - Branched-chain α-keto acid dehydrogenase kinase is responsible for the inactivation and phosphorylation of the branched-chain α-keto acid dehydrogenase complex, the enzyme that catalyses the committed step of branched-chain amino acid catabolism. The activity of the branched-chain α-keto acid dehydrogenase complex is inversely correlated with kinase activity, suggesting that the relative activity of the kinase is the primary regulator of the activity of the complex. It has been shown that kinase activity and expression are affected by nutritional states imposed by low-protein diet feeding, starvation, diabetes, and exercise. Evidence has also been presented that certain hormones, particularly insulin, glucocorticoid, thyroid hormone and female sex hormones, affect the activity and expression of the kinase. The findings indicate that nutritional and hormonal control of the activity and expression of branched-chain α-keto acid dehydrogenase kinase provides an important means of control of the activity of the branched-chain α-keto acid dehydrogenase complex, with inactivation serving to conserve branched-chain amino acids for protein synthesis in some situations and activation serving to provide carbon for gluconeogenesis in others.

AB - Branched-chain α-keto acid dehydrogenase kinase is responsible for the inactivation and phosphorylation of the branched-chain α-keto acid dehydrogenase complex, the enzyme that catalyses the committed step of branched-chain amino acid catabolism. The activity of the branched-chain α-keto acid dehydrogenase complex is inversely correlated with kinase activity, suggesting that the relative activity of the kinase is the primary regulator of the activity of the complex. It has been shown that kinase activity and expression are affected by nutritional states imposed by low-protein diet feeding, starvation, diabetes, and exercise. Evidence has also been presented that certain hormones, particularly insulin, glucocorticoid, thyroid hormone and female sex hormones, affect the activity and expression of the kinase. The findings indicate that nutritional and hormonal control of the activity and expression of branched-chain α-keto acid dehydrogenase kinase provides an important means of control of the activity of the branched-chain α-keto acid dehydrogenase complex, with inactivation serving to conserve branched-chain amino acids for protein synthesis in some situations and activation serving to provide carbon for gluconeogenesis in others.

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