Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems
Covers enzyme kinetics from its most elementary aspects to such modern subjects as steady-state, multi-reactant kinetics and isotope exchange. Offers an understanding of the behavior of enzyme systems and the diagnostic tools used to characterize them and determine kinetic mechanisms. Illustrates and explains current subjects such as cumulative, concerted and cooperative feedback inhibition and metal ion activation.
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affinity allosteric assay assumed binding constants Biochem Biol calculated catalytically active Chapter Chem competitive inhibitor complex cooperative binding cooperativity cosubstrate decreases denominator derived described determined different fixed concentrations dissociation constant Dixon plot effect effector energy charge Enzyme Kinetics enzyme species equal example family of reciprocal Fmax four-site enzyme fraction Henri-Michaelis-Menten equation Hill equation Hill plot hyperbolic I]-axis increases infinitely high inflection point inhibition systems inhibitor concentration inhibitor with respect initial velocity interaction factors intercept versus intersect Koshland ligand binding mixed-type inhibition napp noncompetitive inhibition obtained oligomer partial competitive presence protein pure noncompetitive Rapid Equilibrium Random rate constant rate equation ratio reaction rearranged reciprocal plot replot represents shown in Figure sigmoidal slope specific steady-state substrate inhibition subunit tion two-site varied ligand velocity curve velocity equation versus 1/[S Vmax Vmmx Vmtx y-axis intercept yield zero