A Study of Enzymes, Volume 1

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CRC Press, Nov 21, 1990 - Medical - 488 pages
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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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Contents

Enzyme Catalysis and SteadyState Kinetics
1
Some Elementary Considerations of Enzyme Kinetics
10
Chapter
11
Appendix
15
Hydrolases Mechanisms
22
Effect of Temperature
37
Kinetics of Immobilized Enzymes
47
Chapter 2
57
Chapter 7
283
Chapter 4
296
Chapter 8
301
Case of Multiple Classes of Binding Sites
308
Metalloenzymes
314
Equilibrium Substrate Binding as Illustrated by the ATPTransphosphorylase
317
Structural Relationships of the NucleotideMagnesium Complexes
336
Chapter 9
341

Mechanistic Role of Biotin in Enzymatic Carboxylation Reactions
105
Chapter 3
139
Chapter 4
163
Effect of Temperature on the Reaction Velocity
180
Chapter 5
191
SteadyState Kinetic Analysis of KinaseType of Catalyzed Reactions
212
Chapter 15
222
Chapter 16
236
Calculations of the Equilibrium Concentrations of the Various Ionic
238
Derivation of Equations 20 and 24 from Chapter 1 Corresponding to
245
Enzyme Kinetics and Substrate Binding
251
Kinetic Isotope Effects
262
B Hybrid and Mixed Mechanisms
352
Treatment of Enzyme Kinetic Data
359
ProteasesStructures and Mechanisms
374
Chapter 10
377
Dehydrogenases Structure and Catalytic Mechanisms
384
Rapid Flow Methods
386
Chapter 8
398
Relaxation Methods
401
Concluding Remarks
412
References
419
Index
457
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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.
Page 452 - Craik CS, Largman C, Fletcher T, Roczniak S, Barr PJ, Fletterick R, Rutter WJ (1985) Science 228: 291 40.
Page 453 - T. (1989). Protein hydroxylation: Prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit, FASEB J. 3, 1609-1617.

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