Thiamine: Catalytic Mechanisms in Normal and Disease States, 1st Edition (Hardback) book cover

Thiamine

Catalytic Mechanisms in Normal and Disease States, 1st Edition

Edited by Frank Jordan, Mulchand S. Patel

CRC Press

600 pages

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Hardback: 9780824740627
pub: 2003-12-11
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pub: 2003-12-11
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Description

Thiamine: Catalytic Mechanisms in Normal and Disease States brings together the most recent developments in thiamine diphosphate (TDP)-requiring enzyme research and details the mechanisms of catalysis and structure-function relationships, as well as pathophysiological aspects of a spectrum of diseases associated with TDP-requiring enzymes. Providing new insights into neurogenerative diseases, this volume associates defects in the function of TDP-dependent enzymes with numerous metabolic disorders and disease states and offers novel aspects of thiamine enzymes in chiral synthesis as well as new perspectives on the cellular role of thiamine triphosphate and thiamine triphosphates.

Table of Contents

Chemical Intermediates in Catalysis by Thiamine Diphosphate, Perry A. Frey; Mechanistic and Structural Studies on Thiamine Biosynthetic Enzymes, Tadhg P. Begley and Steven E. Ealick; Studies on the Structure and Function of Thiamine Pyrophosphokinase, Jing-Yuan Liu, David E. Timm, Robert A. Harris and Thomas D. Hurley; New Perspectives on the Cellular Role of Thiamine Triphosphate and Thiamine Triphosphatase, Lucien Bettendorff and Pierre Wins; How Thiamine Works in Enzymes - Time-Resolved NMR Snapshots of ThDP-Dependent Enzymes in Action, Kai Tittmann, Ralph Golbik, Kathrin Uhlemann, Ludmila Khailova, Mulchand Patel, Frank Jordan, David Chipman, Ronald G. Duggleby and Gerhard H bner; Thiamine-Dependent Enzymes as Catalysts of C-C-Bonding Reactions - The Role of Orphan Enzymes, Michael Muller and Georg A. Sprenger; Ligand-Induced Conformational Changes in Thiamine Diphosphate-Dependent Enzymes - Comparison Between Crystal and Solution Structures, Stephan Konig, Michael Spinka, Erik Fiedler, Georg Wille, Johanna Brauer, Michel H.J. Koch and Dmitri I. Svergun; Enantioselective Synthesis of Hydroxy Ketones via Benzaldehyde Lyase- and Benzoylformate Decarboxylase-Catalyzed C-C Bond Formation, Bettina Lingen, Andreas Liese and Michael Muller; Benzoylformate Decarboxylase - Lessons in Enzymology, Michael J. McLeish, George L. Kenyon, Elena S. Polovnikova, Asim K. Bera, Natalie L. Anderson and Miriam S. Hasson; New Concept on the Nature of the Induced Absorption Band of Holotransketolase, Marina V. Kovina, Irina A. Bykova, Olga N. Solovjeva, Ludmilla E. Meshalkina and German A. Kochetov; Structure of the a-Carbanion/Enamine Reaction Intermediate in the Active Site of Transketolase, Determined by Kinetic Crystallography, Tatyana Sandalova, Erik Fiedler, Stina Thorell, Ralph Golbik, Stephan Konig and Gunter Schneider; Yeast Pyruvate Decarboxylase - New Features of the Structure and Mechanisms, Frank Jordan, Min Liu, Eduard Sergienko, Zhen Zhang, Andrew Brunskill, Palaniappa Arjunan and William Furey; Solvent and Carbon Kinetic Isotope Effects on Active-Site and Regulatory-Site Variants of Yeast Pyruvate Decarboxylase, Wen Wei, Min Liu, Lan Chen, W. Phillip Huskey and Frank Jordan; Insights into the Mechanism and Regulation of Bacterial Acetohydroxyacid Synthases, David M. Chipman, Ze'ev Barak, Stanislav Engel, Sharon Mendel and Maria Vyazmensky; Structure and Properties of Acetohydroxyacid Synthase, Ronald G. Duggleby, Luke W. Guddat and Siew Siew Pang; Exploring the Substrate Specificity of Benzoylformate Decarboxylase, Pyruvate Decarboxylase, and Benzaldehyde Lyase, Poetra Siegert, Martina Pohl, Malea M. Kneen, Irina D. Pogozheva, George L. Kenyon and Michael J. McLeish; Benzoylformate Decarboxylase - Intermediates, Transition States, and Diversions, Ronald Kluger, Qingyan Hu and Ian F. Moore; Structural and Functional Organization of Pyruvate Dehydrogenase Complexes, Z. Hong Zhou, Lester Reed and James K. Stoops.

About the Series

Oxidative Stress and Disease

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Subject Categories

BISAC Subject Codes/Headings:
MED008000
MEDICAL / Biochemistry
MED060000
MEDICAL / Nutrition