TY - CHAP M1 - Book, Section TI - Enzymes: Kinetics A1 - Rodwell, Victor W. A2 - Rodwell, Victor W. A2 - Bender, David A. A2 - Botham, Kathleen M. A2 - Kennelly, Peter J. A2 - Weil, P. Anthony PY - 2018 T2 - Harper's Illustrated Biochemistry, 31e AB - OBJECTIVESAfter studying this chapter, you should be able to:Describe the scope and objectives of enzyme kinetic analysis.Indicate whether ΔG, the overall change in free energy for a reaction, is dependent on reaction mechanism.Indicate whether ΔG is a function of the rates of reactions.Explain the relationship between Keq, concentrations of substrates and products at equilibrium, and the ratio of the rate constants k1/k–1.Outline how the concentration of hydrogen ions, of enzyme, and of substrate affect the rate of an enzyme-catalyzed reaction.Utilize collision theory to explain how temperature affects the rate of a chemical reaction.Define initial rate conditions and explain the advantage obtained from measuring the velocity of an enzyme-catalyzed reaction under these conditions.Describe the application of linear forms of the Michaelis-Menten equation to estimate Km and Vmax.Give one reason why a linear form of the Hill equation is used to evaluate how substrate-binding influences the kinetic behavior of certain multimeric enzymes.Contrast the effects of an increasing concentration of substrate on the kinetics of simple competitive and noncompetitive inhibition.Describe how substrates add to, and products depart from, an enzyme that follows a ping-pong mechanism.Describe how substrates add to, and products depart from, an enzyme that follows a rapid-equilibrium mechanism.Provide examples of the utility of enzyme kinetics in ascertaining the mode of action of drugs. SN - PB - McGraw-Hill Education CY - New York, NY Y2 - 2024/03/28 UR - accessmedicine.mhmedical.com/content.aspx?aid=1160189241 ER -