By: J Kyte
540 pages, Figs, tabs
This book examines the chemical methods used to study the mechanisms of enzymatically catalyzed reactions with an emphasis on the crystallographic molecular models of active sites. The book traces the development of enzymatic mechanisms from physical organic studies of nonenzymatic catalysis through detailed examination of the specific interactions between catalytic amino acids and intermediate analogues in crystallographic molecular models. The strategies of enzymatic catalysis, such as coenzymatic assistance, approximation, strain, the use of general acid-bases, the involvement of intermediates, and conformational control, are the central topics around which the book is organized. "The modern standard against which both graduate and reference texts will be judged". -- Paul A. Bartlett, University of California, Berkeley "Indispensable for the serious student of enzyme catalysis and a splendid resource for investigators in the field". -- Paul D. Bayer, University of California, Los Angeles, Emeritus
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