Enzyme Structure and Mechanism

This book explores the mechanisms of enzyme catalysis and specificity, from both the theoretical and experimental points of view. The emphasis is on kinetics and chemical thermodynamics as methods for establishing mechanisms at the atomic level for enzymes whose tertiary structure has already been solved by X-ray crystallography. Those with a good grasp of first-year organic chemistry, physical chemistry, and introductory biochemistry will find that this book starts where their basic courses left off, with a review of catalytic mechanisms and the equations of enzyme kinetics, and then moves into such topics as pre-steady-state kinetics and experimental methods, pH dependence, enzyme-substrate complementarity, and specificity. One chapter is devoted to explaining in detail how kinetic experiments have helped elucidate the mechanisms of selected enzymes by means of the detection of intermediates; the author is careful to discuss what constitutes proof that a certain substance is an intermediate, and reviews sources of possible experimental error. Although the book contains little on multi-substrate systems or on the methods of structure determination themselves, it is nevertheless a well-written, compact introduction to an important field.