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Lecture16 - Lecture 16 Background reading Berg et al Pages...

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Lecture 16 11/2/11 Assignment: Segel: Page 319: problems 2, 6, 7 Background reading: Berg, et al: Pages 238 – 240 Garrett and Grisham: Pages 417 – 419 and 421 - 423 Outline: V max and K M Lineweaver-Burk plot Enzyme inhibition Competitive inhibition
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In the last lecture we derived the Michaelis-Menten equation that describes the hyperbolic curve we get by plotting initial velocity (v o ) as a function of [S]: v = V max [S] K M + S Can use this equation to calculate points on the curve. V max and K M When the [S] >> K M (Greater than 100 x K M ): The K M is small and drops out and the equation becomes v = V max P O Get Zero order kinetics in which the rate of reaction is independent of [S]. When the [S] << K M (Less than .01 x K M ): v = V max [S] K M = k [S] Get First order kinetics in which the velocity is directly proportional to the [S] and the line is straight. If v = ½ the V max the K M = [S] Thus the K M is equal to the substrate concentration at which the reaction rate is half its maximal value.
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