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by M.S. Patel,T.E. Roche,R.A. Harris
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Biological Sciences
  • Author:
    M.S. Patel,T.E. Roche,R.A. Harris
  • ISBN:
    3764351810
  • ISBN13:
    978-3764351816
  • Genre:
  • Publisher:
    Birkhäuser; 1996 edition (February 29, 1996)
  • Pages:
    321 pages
  • Subcategory:
    Biological Sciences
  • Language:
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Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation.

Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies.

Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles . Alpha-Keto Acid Dehydrogenase Complexes.

Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in. .Molecular and Cell Biology Updates. Regulation of branched-chain α-keto acid dehydrogenase complex in rat liver and skeletal muscle by exercise and nutrition.

The hepatic branched-chain alpha-ketoacid dehydrogenase complex plays an important role in regulating branched-chain amino acid levels. These compounds are essential for protein synthesis but toxic if present in excess

The hepatic branched-chain alpha-ketoacid dehydrogenase complex plays an important role in regulating branched-chain amino acid levels. These compounds are essential for protein synthesis but toxic if present in excess. When dietary protein is deficient, the hepatic enzyme is converted to the inactive, phosphorylated state to conserve branched-chain amino acids for protein synthesis. When dietary protein is excessive, the enzyme is in the active, dephosphorylated state to commit the excess branched-chain amino acids to degradation.

a-keto acid dehydrogenase complexes. oceedings{Ishikawa2003aKETOAD, title {a-KETO ACID DEHYDROGENASE COMPLEXES}, author {Eiji Ishikawa and Ibert Oliver and Lester Reed and Clayton}, year {2003} }. Eiji Ishikawa, Ibert Oliver, +1 author Clayton. 1016/0003-9861(72)90152-x. have been isolated as multienzyme complexes with molecular weights of several million from pigeon breast muscle,1' 2 pig heart muscle,3' 4 and Escherichia coli. 5 Two classes of complexes have been obtained, one specific for pyruvate, the other for a-ketoglutarate.

The branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle.

Mulchand S. Patel (Ed. Thomas E. Roche (Ed. 59 international contributors. data. Alpha- Keto Acid Dehydrogenase Complexes Robert A. Harris (Ed., Mulchand S., Thomas E. Birkhäuser, 1996 . catalog. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies employing molecular biology and biophysical techniques. Although these enzyme systems have some features in common, their diversity in fulfilling unique organism - or tissue - specific roles is truly amazing.

Recent application of the tools of molecular biology has provided insight with respect to the structure, regulation, and defects of the genes encoding the PDC and the BCKADC. M S Patel, R A Harris

Recent application of the tools of molecular biology has provided insight with respect to the structure, regulation, and defects of the genes encoding the PDC and the BCKADC. cDNAs for the alpha-KGDC have only recently been cloned. Evidence for long-term regulation of the expression of the subunits of the PDC and the BCKADC has been obtained. Detailed analyses of the promoter-regulatory regions of the genes encoding the individual subunits of these complexes have provided leads as to molecular mechanisms involved. M S Patel, R A Harris. Department of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York at Buffalo 14214, USA.

Branched-chain α-keto acid dehydrogenase complex (BCKDC) is a mitochondrial multienzyme complex that catalyzes a series of reactions that form the first irreversible step in the catabolism of the essential.

Branched-chain α-keto acid dehydrogenase complex (BCKDC) is a mitochondrial multienzyme complex that catalyzes a series of reactions that form the first irreversible step in the catabolism of the essential branched-chain amino acids: leucine, isoleucine, and valine. From: Methods in Enzymology, 2000.

Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies employing molecular biology and biophysical techniques. Although these enzyme systems have some features in common, their diversity in fulfilling unique organism - or tissue - specific roles is truly amazing. These systems have medical importance in areas ranging from defects in regulation (linked to diabetes, heart disease, obesity, nutrition defects), to inherited diseases (inborn errors, maple syrup urine disease) to acquired immune diseases (primary biliary cirrhosis). This book brings together wide-ranging recent findings on the structure(function relationships, gene regulation, and genetic defects of the alpha-keto acid dehydrogenase complexes, namely the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and the branched-chain alpha-keto acid dehydrogenase complexes. A wide variety of experimental approaches together with new results presented in this book should serve as a resource for beginning to established investigators in the field as well as scientists who are interested in mitochondria, dehydrogenases, kinases, phosphatases, lipoic acid, thiamine pyrophosphate, and enzyme complexes.