This enzymology textbook for graduate and advanced undergraduate students covers the syllabi of most universities where this subject is regularly taught. It focuses on the synchrony between the two broad mechanistic facets of enzymology: the chemical and the kinetic, and also highlights the synergy between enzyme structure and mechanism. Designed for self-study, it explains how to plan enzyme experiments and subsequently analyze the data collected. The book is divided into five major sections: 1] Introduction to enzymes, 2] Practical aspects, 3] Kinetic Mechanisms, 4] Chemical Mechanisms, and 5] Enzymology Frontiers. Individual concepts are treated as stand-alone chapters; readers can explore any single concept with minimal cross-referencing to the rest of the book. Further, complex approaches requiring specialized techniques and involved experimentation (beyond the reach of an average laboratory) are covered in theory with suitable references to guide readers. The book provides students, researchers and academics in the broad area of biology with a sound theoretical and practical knowledge of enzymes. It also caters to those who do not have a practicing enzymologist to teach them the subject.

This volume supplements Volumes 63, 64, 87, and 249 of Methods in Enzymology. These volumes provide a basic source for the quantitative interpretation of enzyme rate data and the analysis of enzyme catalysis. Among the major topics covered are Engergetic Coupling in Enzymatic Reactions, Intermediates and Complexes in Catalysis, Detection and Properties of Low Barrier Hydrogen Bonds, Transition State Determination, and Inhibitors.The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.

Kinetic studies of enzyme action provide powerful insights into the underlying mechanisms of catalysis and regulation. These approaches are equally useful in examining the action of newly discovered enzymes and therapeutic agents. Contemporary Enzyme Kinetics and Mechanism, Second Edition presents key articles from Volumes 63, 64, 87, 249, 308 and 354 of Methods in Enzymology. The chapters describe the most essential and widely applied strategies. A set of exercises and problems is included to facilitate mastery of these topics. The book will aid the reader to design, execute, and analyze kinetic experiments on enzymes. Its emphasis on enzyme inhibition will also make it attractive to pharmacologists and pharmaceutical chemists interested in rational drug design.Of the seventeen chapters presented in this new edition, ten did not previously appear in the first edition. - Transient kinetic approaches to enzyme mechanisms - Designing initial rate enzyme assay - Deriving initial velocity and isotope exchange rate equations - Plotting and statistical methods for analyzing rate data - Cooperativity in enzyme function - Reversible enzyme inhibitors as mechanistic probes - Transition-state and multisubstrate inhibitors - Affinity labeling to probe enzyme structure and function - Mechanism-based enzyme inactivators - Isotope exchange methods for elucidating enzymatic catalysis - Kinetic isotope effects in enzyme catalysis - Site-directed mutagenesis in studies of enzyme catalysis

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today—truly an essential publication for researchers in all fields of life sciences. - Spectroscopic Detection of Reaction Intermediates - Isotopic and Kenetic Detection of Reaction Intermediates - Chemical Trapping and Inhibitor Methods for Detecting Reaction Intermediates

Kinetics of Enzyme Catalysis provides an introduction to the fundamentals of understanding an enzyme's catalytic mechanism and how activity is regulated, which is key to understanding biology and many diseases. Kinetics is at the core of enzymology, as it must be for the study of catalysts. Kinetics of Enzyme Catalysis examines simple kinetics and then applies those ideas to enzyme mechanisms, leading to rate equations for several key mechanisms and, as important, illustrating some key principles. A reader should therefore come away empowered with some mathematical tools allowing the analysis of catalytic cycles not discussed here and also with the understanding to predict some behaviors of enzyme kinetics without any math. Methods are discussed in some detail, and with them some considerations for avoiding pitfalls and collecting reliable data. In addition, introductions are presented to the important areas of studying inhibitors, of the origins of the catalytic power of enzymes, and the use of rapid-reaction technology.

First published in 1990, this comprehensive monograph consists of two parts: Volume I, entitled Enzyme Catalysis, Kinetics, and Substrate Binding; and Volume II, entitled Mechanism of Enzyme Action. Volume I focuses on several aspects of enzyme catalytic behavior, their steady-state and transient-state kinetics, and the thermodynamic properties of substrate binding. Packed with figures, tables, schemes, and photographs, this volume contains over 1,000 references, including references regarding enzymology's fascinating history. This comprehensive book is of particular interest to enzymology students, teachers, and researchers. Volume II presents selected "cutting edge" examples of techniques and approaches being pursued in biochemistry. This up-to-date resource includes 11 chapters, which illustrate important theoretical and practical aspects of enzyme mechanisms. It also features selected examples in which today's most important techniques, ideas, and theories are used to elaborate on the intricate nature of enzyme action mechanisms. This particular volume provides important information for both the novice and the seasoned investigator.

Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, Enzyme Kinetics: Catalysis & Control develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. - Historical analysis of kinetic principles including advanced enzyme science - Provides both theoretical and practical measurements tools - Coverage of single molecular kinetics - Examination of force generation mechanisms - Discussion of organic and inorganic enzyme reactions

Chemistry and chemical technology have been at the heart of the revolutionary developments of the 20th century. The chemical industry has a long history of combining theory (science) and practice (engineering) to create new and useful products. Worldwide, the process industry (which includes chemicals, petrochemicals, petroleum refining, and pharmaceuticals) is a huge, complex, and interconnected global business with an annual production value exceeding 4 trillion dollars. Although in industry special focus is in heterogeneous catalysis, homogeneous, enzymatic, photochemical and electrochemical catalysis should not be overlooked; as the major aim is to produce certain chemicals in the best possible way, applying those types of catalysis, which suit a particular process in the most optimal way. Catalysis according to the very definition of it deals with enhancement of reaction rates, that is, with catalytic kinetics. This book unifies the main sub disciplines forming the cornerstone of catalytic kinetics.* Provides a broad overview catalytic kinetics* Bridges the gaps that exist between hetero-, homo- and bio-catalysis* Written by internationally renowned experts in this field

This volume discusses questions of free-radical biology and new, modern directions in molecular cytobiology; proteomics and genomics. The book presents articles and reviews on bioantioxidants, synthesis of new compounds, mechanisms of their action and areas of application. Studies on free radical states using ESR technique, biochemistry of regulatory systems and the role of free radicals in radiation disease and cancer development are given special attention. Test results of new drugs for curing malignant tumors and kinetic approaches to the description of disease development and estimation of curative action of medicinal preparations are shown. The book also presents studies in the branch of enzymology, receptor systems, photoreception, in particular. The volume uniquely presents general tendencies in chemistry, biology and medicine kinetically united and attached to free radical mechanisms and other questions under consideration.

Kinetic studies of enzyme action provide insights into the underlying mechanisms of catalysis and regulation. This volume presents key articles from Volumes 63, 64, 87 and 249 of "Methods in Enzymology". The chapters describe the most essential and widely applied strategies.