A Study of Enzymes, Volume 1
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.
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Enzyme Catalysis and SteadyState Kinetics
Some Elementary Considerations of Enzyme Kinetics
Effect of Temperature
Kinetics of Immobilized Enzymes
Case of Multiple Classes of Binding Sites
Equilibrium Substrate Binding as Illustrated by the ATPTransphosphorylase
Structural Relationships of the NucleotideMagnesium Complexes
Mechanistic Role of Biotin in Enzymatic Carboxylation Reactions
Effect of Temperature on the Reaction Velocity
SteadyState Kinetic Analysis of KinaseType of Catalyzed Reactions
Calculations of the Equilibrium Concentrations of the Various Ionic
Derivation of Equations 20 and 24 from Chapter 1 Corresponding to
Enzyme Kinetics and Substrate Binding
Kinetic Isotope Effects
acid activated complex adenylate kinase approximately ATP-creatine transphosphorylase Biochemistry Biol brain type calculated calf muscle catalysis catalytic Chapter Chem chemical Cleland coef coefficient competitive inhibitor conformational changes creatine kinase dehydrogenase denominator double-reciprocal plots energy enzyme kinetics equilibrium constant estimated Figure forward reaction glucose 6-phosphate hexokinase initial velocity interaction intercept interconversion intrinsic dissociation constant ionization isoenzymes isotope effects kcal/mol kinetic isotope effects kinetic parameters Kuby ligand linear liver measurements membrane MgADP MgATP molecule muscle enzyme muscle type noncompetitive inhibitor nucleotide obtained ordered BiBi plmol primary plots product inhibition protein proton quasi-equilibrium rabbit muscle rapid equilibrium rate constants reactants reverse reaction Scheme secondary plots slope solution species steady-state studies substrate concentration subunit Table temperature ternary complex Theorell-Chance thermodynamic two-substrate values varied velocity equation velocity expression Vmax Y-int Y-intercept yeast yield
Page 421 - Manual ot its recommended sources. Terminology and classification for enzymes should follow the Commission on Biochemical Nomenclature on the Nomenclature and Classification of Enzymes.