330-10 JP 15

330-10 JP 15 - BISC 330L Sp2010 Lect JP 15.ppt Wednesday,...

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BISC 330L Sp2010 Lect JP 15.ppt Wednesday, 17 Feb 2010 Petruska Lecture 14 (Enzyme Kinetics) Cont’d Lecture 15: Michaelis-Menten Equation, Linear Plots, and Reversible Inhibition Model Reference: BTS (6th ed.) Chap. 8
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Biochemistry Sixth Edition Chapter 8: Enzymes: Basic Concepts and Kinetics Copyright © 2007 by W. H. Freeman and Company   Berg • Tymoczko • Stryer Sections 8.4-8.5: Enzyme Kinetics & Inhibition
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Lock-and-key model of enzyme-substrate binding. (Binding energy holds substrate in pre-formed active site)
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Induced-fit model of enzyme-substrate binding. (Some of the binding energy is needed to form the active site)
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Determining initial velocity (i.e., when [P]<<[S]).
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Curve of v 0 vs. [S] for Michaelis-Menten kinetics
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Michaelis-Menten Model of Enzyme Kinetics Section 8.4 Equation (13), p.217 k 1 k 2 E + S ES E + P k -1 Assumptions: (a) k 2 represents catalytic rate (k cat ) for converting ES to EP, if catalysis is slow compared to P release. (b) k -2 can be ignored as long as [P] << [S],
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Case 1: Binding withou t catalysis (k 2 = 0) ES quickly reaches equilibrium : d[ES] / dt = k 1 [E][S] - k -1 [ES] = 0 at equilibrium Then, k -1 [ES] = k 1 [E][S] (at equilibrium) i.e., k -1 / k 1 = [E][S] / [ES] = K D (or K d ) Eq. 1 where K D = k -1 / k 1 is the equilibrium dissociation constant for ES
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330-10 JP 15 - BISC 330L Sp2010 Lect JP 15.ppt Wednesday,...

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