PS #14 - Oct 11 Answers

PS #14 - Oct 11 Answers - complex, however, the V max is...

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1 What does V max indicate? Ans: The maximum velocity or rate of reaction as catalyzed by a specific amount of enzyme when it is saturated with substrate. 2 What is the upper limit of k cat / K M ? Ans: The diffusion-controlled interaction of the substrate and enzyme determines the upper limit of the rate. The upper limit is 10 8 – 10 9 s -1 M -1 . 3 How are the types of inhibition kinetically distinguishable? Ans: Competitive inhibition can be overcome by the presence of large amounts of substrate. However, the apparent K M is increased. In noncompetitive inhibition, substrate can bind to the EI
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Unformatted text preview: complex, however, the V max is decreased. In mixed inhibition, both values may be altered. 4 In an enzymatic reaction in a test tube, the reaction will eventually reach equilibrium. Why does this not happen in living organisms? Ans: In a cell, the product may be utilized for a subsequent reaction, thus the reaction may not reach equilibrium. 5 What is the Michaelis-Menten equation? Define all parameters. Ans: V = V max (S/(S + K M )) Initial velocity V Maximum velocity V max Substrate concentration S Michaelis constant K M...
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This note was uploaded on 01/25/2010 for the course SCIENCE bioc300 taught by Professor Foster during the Spring '10 term at UBC.

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