Enzyme Kinetics: A Modern ApproachPractical Enzyme Kinetics provides a practical how-to guide for beginning students, technicians, and non-specialists for evaluating enzyme kinetics using common software packages to perform easy enzymatic analyses. |
Contents
| 1 | |
2 HOW DO ENZYMES WORK? | 41 |
3 CHARACTERIZATION OF ENZYME ACTIVITY | 44 |
4 REVERSIBLE ENZYME INHIBITION | 61 |
5 IRREVERSIBLE ENZYME INHIBITION | 70 |
6 pH DEPENDENCE OF ENZYMECATALYZED REACTIONS | 79 |
7 TWOSUBSTRATE REACTIONS | 90 |
8 MULTISITE AND COOPERATIVE ENZYMES | 102 |
10 INTERFACIAL ENZYMES | 121 |
11 TRANSIENT PHASES OF ENZYMATIC REACTIONS | 129 |
12 CHARACTERIZATION OF ENZYME STABILITY | 140 |
13 MECHANISMBASED INHIBITION | 158 |
14 PUTTING KINETIC PRINCIPLES INTO PRACTICE | 174 |
15 USE OF ENZYME KINETIC DATA IN THE STUDY OF STRUCTUREFUNCTION RELATIONSHIPS OF PROTEINS | 193 |
| 217 | |
| 221 | |
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Common terms and phrases
allosteric alternate substrate amino acid assay bimolecular calculated catalysis catalytic parameters changes cooperative enzyme corresponds data points data set decimal reduction decrease denaturation determined differential equation dissociation constant energy of activation enzymatic reaction enzyme activity enzyme kinetic enzyme mass balance enzyme stability enzyme-catalyzed reaction enzyme–inhibitor complex equilibrium constant estimates of Vmax experimental data expression Figure free enzyme function Hill equation increase Initial velocity versus integrated rate equation interfacial enzyme kcat kobs linear plot Lys36pArg Lys36pMet mechanism Michaelis–Menten model mutations N-frag(A N-terminal nonlinear regression obtain estimates pepsin pepsinogen pH dependence pK values possible to obtain progress curve prosegment protein rate constant rate equation rate of inhibition reaction rate reaction velocity reactive rearrangement residues second-order slope standard-state steady-state substrate binding substrate inhibition suicide inhibitor temperature tion total enzyme concentration Trx-PG V∗max van’t Hoff equation velocity versus substrate versus substrate concentration wild-type y-intercept yields a straight
Popular passages
Page 217 - Kinetics of Chemical and Enzyme-Catalyzed Reactions, Oxford University Press, New York, 1977. Plowman, KM, Enzyme Kinetics, McGraw-Hill, New York, 1972. Purich, DL, Ed., Enzyme Kinetics and Mechanism Part D, Developments in Enzyme Dynamics, Methods in Enzymology, Vol.
Page 217 - Determining the chemical mechanisms of enzymecatalyzed reactions by kinetic studies, Adv.
Page xvi - A + B — > C. The Law of Mass Action states that the rate at which (' is formed is proportional to the product of the quantities of A and B present.