Download Alpha-Keto Acid Dehydrogenase Complexes by R. N. Perham (auth.), Prof. Mulchand S. Patel, Dr. Thomas E. PDF

By R. N. Perham (auth.), Prof. Mulchand S. Patel, Dr. Thomas E. Roche, Dr. Robert A. Harris (eds.)

Found in all organisms, the alpha-keto acid dehydrogenase complexes have imperative roles in mobile metabolism and are significant websites of rules. the knowledge of the association, functionality and legislation of those crucial multienzyme complexes has been significantly complex via experiences using molecular biology and biophysical ideas. even if those enzyme platforms have a few positive factors in universal, their variety in gratifying targeted organism - or tissue - particular roles is actually outstanding. those structures have scientific significance in components starting from defects in rules (linked to diabetes, center illness, weight problems, foodstuff defects), to inherited illnesses (inborn error, maple syrup urine affliction) to got immune illnesses (primary biliary cirrhosis). This e-book brings jointly wide-ranging fresh findings at the structure(function relationships, gene law, and genetic defects of the alpha-keto acid dehydrogenase complexes, specifically the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and the branched-chain alpha-keto acid dehydrogenase complexes. a large choice of experimental ways including new effects offered during this ebook may still function a source for commencing to tested investigators within the box in addition to scientists who're drawn to mitochondria, dehydrogenases, kinases, phosphatases, lipoic acid, thiamine pyrophosphate, and enzyme complexes.

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R Acyl-CoA Fat l

G. S. (1995) Mutagenic studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation. J. Bioi. Chem. 270: 14297 -14304. , Kim, H. S. (1995) Overexpression and characterization of human tetrarneric pyruvate dehydrogenase and its individual subunits. Prot. Express. Purif. 6: 79-90. AD. N. (1994) Expression in Escherichia coli of genes encoding the Ela and EIJ3 subunits of the pyruvate dehydrogenase complex of Bacillus stearotherrnophilus and assembly of a functional El component (a2J32) in vitro.

Biochem. Biophys. Res. Comm. 164: 941-946. I. o. (1990) Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner. Proc. Natl. Acad. Sci. USA 87: 673-676. F. I. (1977) Binding of thiamin thiazolone pyrophosphate to mammalian pyruvate dehydrogenase and its effects on kinase and phosphatase activities. 1. BioI. Chem. 74: 16671674. M. G. (1994) Investigation of the cofactor-binding site of Zymomonas mobilis pyruvate decarboxylase by site-directed mutagenesis.

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