6-25 For Umax 57(Kr+S) constant an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM b) c) d) e) [S] = 0.5KM [S] = 0.1 KM [S] = 2KM = [S] 10KM Gener (liction)) Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
6-25 For Umax 57(Kr+S) constant an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM b) c) d) e) [S] = 0.5KM [S] = 0.1 KM [S] = 2KM = [S] 10KM Gener (liction)) Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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The Michaelis Menton equation
For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative relationship between the initial velocity (vo), maximum velocity(vmax), the initial substrate concentration ([S]) and enzyme's affinity(Km).
Michaelis Menton equation --> vo = Vmax · [S] / (Km + [S])
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