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 significant roles in mobile metabolism and are significant websites of law. the certainty of the association, functionality and law of those crucial multienzyme complexes has been enormously complex via reports making use of molecular biology and biophysical strategies. even though those enzyme structures have a few good points in universal, their range in enjoyable distinctive organism - or tissue - particular roles is actually notable. those platforms have clinical value in parts starting from defects in rules (linked to diabetes, center affliction, weight problems, foodstuff defects), to inherited ailments (inborn mistakes, maple syrup urine ailment) to got immune ailments (primary biliary cirrhosis). This ebook brings jointly wide-ranging contemporary 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 methods including new effects awarded during this e-book should still function a source for commencing 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 info for Alpha-Keto Acid Dehydrogenase Complexes
I. (1978) Regulation of pig heart pyruvate dehydrogenase by phosphorylation. Studies on the subunit and phosphorylation stoichiometries. Biochem. J. 173: 659-668. A. M (1979) Amino acid sequences around the sites of phosphorylation in the pig heart pyruvate dehydrogenase complex. Biochem. J. 181: 419-426. I. J. (1979) Function of phosphorylation sites on pyruvate dehydrogenase. Biochem. Biophys. Res. Comm. 87: 244-252. Thissen, J. and Komuniecki, R. (1988) Phosphorylation and inactivation of the pyruvate dehydrogenase from anaerobic parasitic nematode, Ascaris suum.
40 la Figure 4. Model of the domains of an E2 subunit binding an a~ unit of the E I component by its B domain and a kinase subunit by its L2 domain plus the inner part of the Jipoyl prosthetic group of L2. In the upper section the model depicts hinge connected Ll and L2 domains with attached Jipoyl groups. A major portion of L2 and the inner part of its lipoyl-Iysine side chain are positioned under (dashed lines) and interacting with a kinase subunit (K). The ~ subunit of E I interacts with the B domain of E2 and the a subunit of E I is positioned to serve as a substrate for the kinase subunit.
Again stimulation by acetyl-CoA required E2r to catalyze acetylation along with addition to Ll or L2. Figure 6 models this L2-mediated signal translation regulation for changes in kinase activity in response to changes in the product-to-substrate ratios. The kinase is converted from a non stimulated (K) to partially activated (K*) to fully stimulated (K**) due to interacting with L2 with oxidized, reduced, or reductively acetylated lipoates, with the latter interaction being favored based on the following findings.