Chemical catalysis (transition state theory, principles of catalysis, covalent catalysis, kinetic isotope effect); Enzyme catalysis; The basic equations of enzyme kinetics (steady-state kinetics, Michaelis-Menten model, inhibition, multisubstrate systems); Measurements and magnitude of individual rate constants (conventional methods, rapid methods-stopped flow, relaxation, quenching, analysis of pre-steady state and relaxation kinetics); The pH dependence of enzyme catalysis; Practical methods for kinetics and equilibria; Detection of intermediates in enzymatic reactions; Irreversible inhibition; Allosteric interactions (positive and negative cooperativity, Hill equation); Stereochemistry of enzymatic reactions; Enzyme-substrate complementarity and the use of binding energy in catalysis; Specificity of enzyme catalysis (limits on specificity; editing or proofreading mechanisms); Catalytic RNA; Selected examples of enzymatic reactions.
D. L. Nelson, M. M. Cox, Lehninger principles of biochemistry, W. H. Freeman & Co., 7th ed. New York, 2017.
Fersht, Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, W. E. Freeman and Company, New York, 1999.
Cornish-Bowden, Fundamentals of Enzyme Kinetics, Portland Press, London, 2004.
H. Segel, Enzyme Kinetics : Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems, Wiley Classics Library Edition, 1993
- ADDITIONAL LITERATURE:
D.L. Purich, Enzyme kinetics: Catalysis and Control, Elsevier Inc, 2010
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