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 legislation. the certainty of the association, functionality and rules of those indispensable multienzyme complexes has been significantly complex through reports using molecular biology and biophysical options. even though those enzyme structures have a few gains in universal, their variety in enjoyable targeted organism - or tissue - particular roles is really remarkable. those platforms have scientific value in parts starting from defects in rules (linked to diabetes, center illness, weight problems, meals defects), to inherited illnesses (inborn error, maple syrup urine disorder) to got 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 e-book should still function a source for commencing to validated 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

Sample text

I I ~ I . " ...... -I " •• ' - NAD+ ~,,' • ... '. '. '. r Acyl-CoA Fat l

T) testis-specific form ofEla. , 1989). , 1990). The corresponding sequence for Escherichia coli EI is completely different (it has structure of a2 dimer) and there is no regulation by covalent modification. Plants have PDC in mitochondria and plastid, and both of them are regulated by phosphorylationdephosphorylation; this regulation also depends upon light (Budde and Randall, 1990). The role of individual phosphorylation sites in regulation of mammalian EI has not been well defined. , 1978; Kerbey and Randle, 1985).

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. J. Bioi. 269: 10378-10383. , Errnler, U. and Sundstrom, M. 5 A. resolution. EMBO J. 11: 2373 - 2379. H. J. (1969) a-Keto acid dehydrogenase complexes.

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