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The kinetics analyses of an enzyme are measured as a function of substrate concentration in the presence and in the absence of 2mM inhibitor (I).
[S] (µM): 3, 5, 10, 30, 90
Velocity (µmol/min) No Inhibitor: 10.4, 14.5, 22.5, 33.8, 40.5
Velocity (µmol/min) With Inhibitor: 4.1, 6.4, 11.3, 22.6, 33.8
(a) What are the values of Vmax and Km in the absence of inhibitor? In its presence?(b) What type of inhibition is it?(c) What is the Ki of the inhibitor?(d) Is [S] = 10µM and [I] = 2mM, what fraction of the enzyme molecules have a bound substrate? A bound inhibitor?
Calculate how the permeability of each is altered when the pH is reduced to 1.0, a value typical of the stomach.How to demolish the function of this protein.
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he p K 1 , p K 2 , and pK R of the amino acid lysine are 2.2, 9.1, and 10.5, respectively. The p K 1 , p K 2 , and pK R of the amino acid arginine are 1.8, 9.0, and 12.5, respectively
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Determine a news report of a current outbreak or other health crisis (within a month) then search for a peer-reviewed scientific article on the same or closely related topic
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