Lecture15

Lecture15 - Lecture 15 10/31/11 HAPPY HALLOWEEN !...

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Lecture 15 10/31/11 HAPPY HALLOWEEN !!! Background reading: Berg, et al: Pages 230 - 234 Garrett and Grisham: Pages 412 - 416 Outline: Michaelis-Menten equation Rapid equilibrium approach Steady-state approach
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The effect of the substrate concentration on the initial velocity of an enzyme-catalyzed reaction suggested the formation of an enzyme-substrate complex occurs as a first step in the catalysis of a reaction. Michaelis-Menten equation E + S ES E + P k -1 k 1 k 2 E + S ES E + P k -1 k 1 k 2 k -2 In 1913, Michaelis and Menten developed a general theory for enzyme action that describes the above curve. They used a rapid equilibrium approach that assumed a rapid equilibrium between E + S ES compared to ES E + P. Thus the velocity at any time depends on [ES].
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Rapid equilibrium approach Since we assume that the ES E + P reaction is insignificant since we are dealing with initial velocity v = k p [ES] [E T ] = [E] + [ES] If divide both sides by [E T ] v [E T ] = k p [ES] [E] + [ES] Because of the equilibrium assumption, can express [ES] in
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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Lecture15 - Lecture 15 10/31/11 HAPPY HALLOWEEN !...

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