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 primary roles in mobile metabolism and are significant websites of rules. the knowledge of the association, functionality and law of those necessary multienzyme complexes has been vastly complex by way of experiences applying molecular biology and biophysical options. even supposing those enzyme platforms have a few gains in universal, their variety in satisfying specific organism - or tissue - particular roles is actually outstanding. those platforms have scientific significance in parts starting from defects in law (linked to diabetes, middle ailment, weight problems, nutrients defects), to inherited ailments (inborn error, maple syrup urine sickness) to received immune illnesses (primary biliary cirrhosis). This e-book brings jointly wide-ranging contemporary findings at the structure(function relationships, gene legislation, 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 techniques including new effects offered during this publication may still function a source for starting to proven 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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Additional resources for Alpha-Keto Acid Dehydrogenase Complexes
207: 437 -444. J. (1974) Multienzyme complexes. Acc. Chem. Res. 7: 40-46. H. and Chun, K. (1993) The relationship between transketolase, yeast pyruvate decarhoxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex. FEBS Lett. 328: 99-102. E. I. (1972) Function of the nonidentical subunits of mammalian pyruvate dehydrogenase. Biochem. Biophys. Res. Comm. 48: 840-846. S. R. (1992) Overproduction of the pyruvate dehydrogenase multienzyme complex of Escherichia coli and site-directed substitutions in the Elp and E2p subunits.
The three-dimensional structure of E 1 will provide new directions for the more detailed investigations of the El active site. S. Public Health Service Grant DK20478. E. S. (\993) Identification of the essential cysteine residue in the active site of bovine pyruvate dehydrogenase. J. Bioi. Chern. 268: 22353-22356. 30 L. G. Korotchkina et al. E. S (1995) Identification of the tryptophan residue in the thiamin pyrophosphate binding site of bovine pyruvate dehydrogenase. 1. Bioi. Chem. 270: 4570-4574.
S. E. A. E. Roche, S. Liu, S. Ravindran, lC. Baker and L. Wang Department of Biochemistry, Kansas State University, Manhattan, KS 66506, USA System and feedback regulation The mammalian pyruvate dehydrogenase complex (PDC) is a large assembly composed of six components with nine distinct subunits. Four of these components execute the overall reaction through a series of steps linked by cofactor-mediated active site coupling: the pyruvate dehydrogenase component (E1); the dihydrolipoyl acetyltransferase component (E2); the dihydro\ipoy\ dehydrogenase component (E3); and the E3-binding component (E3BP, previously protein X) (reviewed: Patel and Roche, 1990; Reed and Hackert, 1990; Perham, 1991).
Alpha-Keto Acid Dehydrogenase Complexes by R. N. Perham (auth.), Prof. Mulchand S. Patel, Dr. Thomas E. Roche, Dr. Robert A. Harris (eds.)