Enzyme Kinetics and MechanismEnzyme Kinetics and Mechanism is a comprehensive textbook on steady-state enzyme kinetics. Organized according to the experimental process, the text covers kinetic mechanism, relative rates of steps along the reaction pathway, and chemical mechanism-including acid-base chemistry and transition state structure. Practical examples taken from the literature demonstrate theory throughout. The book also features numerous general experimental protocols and how-to explanations for interpreting kinetic data. Written in clear, accessible language, the book will enable graduate students well-versed in biochemistry to understand and describe data at the fundamental level. Enzymologists and molecular biologists will find the text a useful reference. |
Contents
Nomenclature | 1 |
Introduction to Kinetics | 9 |
Enzyme Assays | 19 |
Copyright | |
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13C isotope effect acid allosteric apparent aspartate asymptote bireactant catalyzes coef combination competitive inhibition dead-end inhibitor decreases denominator determined deuterated deuterium deuterium isotope effect dissociation constant double reciprocal plot enzyme form equal equilibrium constant equilibrium isotope effect equilibrium ordered example Figure formation given in equation gives half-reaction hexokinase increases inhibition by Q inhibition constant initial rate initial velocity pattern K₁ k₁A k₂ Kia Kb kinase kinetic mechanism labeled levels liver alcohol dehydrogenase malate measured method MgATP Michaelis constant NADH noncompetitive inhibition observed obtained oxaloacetate pathway Ping Pong mechanism pK₁ proline racemase proton random mechanism rapid equilibrium random rate constant rate equation rate-limiting ratio reactant reactant concentration reverse saturating shown in equation slope and intercept slow binding step sticky substrate concentration substrate inhibition term tritium unlabeled V₁ varied reactant varied substrate zero