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 important roles in mobile metabolism and are significant websites of rules. the certainty of the association, functionality and rules of those fundamental multienzyme complexes has been significantly complicated via reports making use of molecular biology and biophysical options. even if those enzyme platforms have a few beneficial properties in universal, their variety in satisfying precise organism - or tissue - particular roles is actually impressive. those structures have clinical significance in components starting from defects in rules (linked to diabetes, middle illness, weight problems, nutrients defects), to inherited illnesses (inborn blunders, maple syrup urine ailment) to obtained immune illnesses (primary biliary cirrhosis). This ebook brings jointly wide-ranging contemporary findings at the structure(function relationships, gene legislation, and genetic defects of the alpha-keto acid dehydrogenase complexes, particularly the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and the branched-chain alpha-keto acid dehydrogenase complexes. a wide selection of experimental ways including new effects provided during this e-book may still function a source for starting to tested investigators within the box in addition to scientists who're attracted to mitochondria, dehydrogenases, kinases, phosphatases, lipoic acid, thiamine pyrophosphate, and enzyme complexes.

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Chem. 263: 119092-19097. 32 L. G. Korotchkina et al. -Y. 1. (1986) Phosphorylation-dephosphorylation of pyruvate dehydrogenase from baker's yeast. Biochemistry 25: 5673-5677. 1. 1. (1976) The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation. Biochem. 1. 157: 4167. G. S. (1991) Sequence conservation in the a and ~ subunits of pyruvate dehydrogenase and its similarity to branched-chain a-keto acid dehydrogenase. FEBS Lett. 282: 209-213.

Here, E1a is used to designate the active fonn of E1 and E1b to designate the phosphorylated, inactive fonn. Figure 1 shows the relationship of PDC reaction and its regulation to other metabolic pathways. In mammalian cells, flux through the PDC reaction controls the oxidative utilization of glucose (Randle, 1986) and results in a net depletion of body carbohydrate reserves by the PDC reaction. The activity of PDC must be reduced when fatty acids or ketone bodies are being preferentially used to provide acetyl-CoA for oxidative energy production by citric acid cycle/oxidative phosphorylation systems - a routine situation in many body organs.

These engage unique organizational and operational features of the pyruvate dehydrogenase complex. The Ela kinase binds very tightly to the E2 core; at the same time, a kinase functional unit (considered below) can rapidly phosphorylate a large complement ofEla tetramers which are bound throughout the complex. We have obtained new insights into the dynamic functioning of the E2 core in support maneuvers that facilitate an efficient seek and tum off operation by the kinase within the complex. Understanding this fundamental operation of the kinase is crucial for appreciating the additional roles of the E2 core in mediating the enhancement of kinase activity in response to increased NADH and acetyl-CoA.

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