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Titlebook: Alpha-Keto Acid Dehydrogenase Complexes; Mulchand S. Patel,Thomas E. Roche,Robert A. Harris Book 1996 Birkhäuser Verlag 1996 Molekularbiol

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发表于 2025-3-21 18:26:14 | 显示全部楼层 |阅读模式
期刊全称Alpha-Keto Acid Dehydrogenase Complexes
影响因子2023Mulchand S. Patel,Thomas E. Roche,Robert A. Harris
视频videohttp://file.papertrans.cn/154/153907/153907.mp4
学科分类Molecular and Cell Biology Updates
图书封面Titlebook: Alpha-Keto Acid Dehydrogenase Complexes; Mulchand S. Patel,Thomas E. Roche,Robert A. Harris Book 1996 Birkhäuser Verlag 1996 Molekularbiol
影响因子Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies employing molecular biology and biophysical techniques. Although these enzyme systems have some features in common, their diversity in fulfilling unique organism - or tissue - specific roles is truly amazing. These systems have medical importance in areas ranging from defects in regulation (linked to diabetes, heart disease, obesity, nutrition defects), to inherited diseases (inborn errors, maple syrup urine disease) to acquired immune diseases (primary biliary cirrhosis). This book brings together wide-ranging recent findings on the structure(function relationships, gene regulation, and genetic defects of the alpha-keto acid dehydrogenase complexes, namely the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and the branched-chain alpha-keto acid dehydrogenase complexes. A wide variety of experimental approaches together with new results presented in this book should serve as a resource
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Probing the active site of mammalian pyruvate dehydrogenase, reactions: the thiamin pyrophosphate (TPP)-dependent decarboxylation of pyruvic acid to 2-hydroxyethylidene-TPP (HETPP) [Eq. 1] and reductive acetylation of lipoic acid residues covalently linked to the second catalytic component — dihydrolipoamide acetyltransferase (E2) [Eq. 2] (Reed, 1974): . Mam
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Role of the E2 core in the dominant mechanisms of regulatory control of mammalian pyruvate dehydrogs 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 dihydrolipoyl dehydrogenase component (E3); and the E3-binding component (E3BP, previously pro
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Plant pyruvate dehydrogenase complexes,uirements have led to increasing diversity between these two classes of eukaryotes. Analyses of the pyruvate dehydrogenase complex (PDC) in plant cells serve to illustrate both the similarities inherent in pyruvate metabolism and differences dictated by the need to respond to diverse external stimul
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,The mitochondrial α-ketoacid dehydrogenase kinases: Molecular cloning, tissue-specific expression arotein kinases (Popov et al., 1992; Popov et al., 1993; Popov et al., 1994). The first of these enzymes to be cloned (Popov et al., 1992), the branched chain α-ketoacid dehydrogenase kinase (BDK), phosphorylates and inactivates the branched-chain α-ketoacid dehydrogenase complex (BCKDC), the rate-li
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