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Enzyme Catalysis and Regulation is an introduction to enzyme catalysis and regulation and covers topics ranging from protein structure and dynamics to steady-state enzyme kinetics, multienzyme complexes, and membrane-bound enzymes. Case studies of selected enzyme mechanisms are also presented. This book consists of 11 chapters and begins with a brief overview of enzyme structure, followed by a discussion on methods of probing enzyme structure such as X-ray crystallography and optical spectroscopy. Kinetic methods are then described, with emphasis on the general principles of steady-state and transient kinetics. The chemical principles involved in enzyme catalysis are also discussed, and case studies of a few well-documented enzymes are presented. The regulation of enzyme activity is analyzed from a nongenetic viewpoint, with particular reference to binding isotherms and models for allosterism. Two particular enzymes, aspartate transcarbamoylase and phosphofructokinase, are used as examples of well-studied regulatory enzymes. The last two chapters focus on multienzyme complexes and membrane-bound enzymes. This monograph is intended for graduate students, advanced undergraduates, and research workers in molecular biology and biochemistry.
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.
The remarkable expansion of information leading to a deeper understanding of enzymes on the molecular level necessitated the development of this volume which not only introduces new topics to The Enzymes series but presents new information on some covered in Volume I and II of this edition.
Exceptionally clear coverage of mechanisms for catalysis, forces in aqueous solution, carbonyl- and acyl-group reactions, practical kinetics, more.
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
Biology for AP® courses covers the scope and sequence requirements of a typical two-semester Advanced Placement® biology course. The text provides comprehensive coverage of foundational research and core biology concepts through an evolutionary lens. Biology for AP® Courses was designed to meet and exceed the requirements of the College Board’s AP® Biology framework while allowing significant flexibility for instructors. Each section of the book includes an introduction based on the AP® curriculum and includes rich features that engage students in scientific practice and AP® test preparation; it also highlights careers and research opportunities in biological sciences.
Christopher M. Cheatum and Amnon Kohen, Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer. Cindy Schulenburg and Donald Hilvert, Protein Conformational Disorder and Enzyme Catalysis. A. Joshua Wand, Veronica R. Moorman and Kyle W. Harpole, A Surprising Role for Conformational Entropy in Protein Function. Travis P. Schrank, James O. Wrabl and Vincent J. Hilser, Conformational Heterogeneity Within the LID Domain Mediates Substrate Binding to Escherichia coli Adenylate Kinase: Function Follows Fluctuations. Buyong Ma and Ruth Nussinov, Structured Crowding and Its Effects on Enzyme Catalysis. Michael D. Daily, Haibo Yu, George N. Phillips Jr and Qiang Cui, Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations. Karunesh Arora and Charles L. Brooks III, Multiple Intermediates, Diverse Conformations, and Cooperative Conformational Changes Underlie the Catalytic Hydride Transfer Reaction of Dihydrofolate Reductase. Steven D. Schwartz, Protein Dynamics and the Enzymatic Reaction Coordinate.
Enzyme Regulation in Metabolic Pathways shows the reader how to understand the roles of enzymes and their kinetic constants in intermediary metabolism. It provides a means of correlating data obtained in experimental studies to multiple possible mechanisms through which some enzyme may catalyze the conversion of a substrate to a product. Although not the most appropriate means of determining some potential kinetic mechanism, quasi-equilibrium assumptions are used throughout the book, keeping the rate equation derivations simple. Actual metabolic pathways with known (presumed) positive and negative regulation events are linked to these potential kinetic mechanisms using both rate equation derivations and data plots illustrating how the rate equation derivations can be used to explain the data plots. This book will be a valuable reference for students in biological sciences and biochemistry majors required to take a core course in enzymology.
The three-dimensional structure of proteins -- Chemical catalysis -- The basic equations of enzyme kinetics -- Measurement and magnitude of individual rate constants -- The pH dependence of enzyme catalysis -- Practical methods for kinetics and equilibria -- Detection of intermediates in enzymatic reactions -- Stereochemistry of enzymatic reactions -- Active-site-directed and enzyme-activated irreversible inhibitors : "affinity labels" and "suicide inhibitors" -- Conformational change, allosteric regulation, motors, and work -- Forces between molecules, and binding energies -- Enzyme-substrate complementarity and the use of binding energy in catalysis -- Specificity and editing mechanisms -- Recombinant DNA technology -- Protein engineering -- Case studies of enzyme structure and mechanism -- Protein stability -- Kinetics of protein folding -- Folding pathways and energy landscapes.