BIOCHEMISTRY QUESTIONThe initial rate (VO) data as a function of substrate concentration [S] for an enzyme (Enzyme1) thatobeys Michaelis-Menten kinetics are shown in the table below. The totalenzyme concentration is 2.5 nM.[S](μm)16.08.04.02.01.0v (μMsec ¹)48.532.719.811.15.88(a) Calculate KM for the enzyme, using the estimated slope (slope = (y2-y1)/(x2-x1)) from aLineweaver-Burk plot. Show your work and don't forget the units!(b) When the enzyme concentration is 2.5 nM, a Lineweaver-Burk plot of this data gives a line with a y-intercept of 0.0106 μ M-1 sec. Calculate kcat for the enzyme. (Show yourwork and don't forget to include units).(c) A second enzyme (Enzyme2) also obeys Michaelis-Menten kinetics. Its kcat and KM are 800 sec-1and 5 µM, respectively. Which is the more efficient enzyme? Briefly explaind) Is Enzyme 1 diffusion limited? Explain.

Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction…

Answered: The initial rate (v0) data as a…

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 KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
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The initial rate (v0) data as a function of substrate concentration [S] for an enzyme (Enzyme1) that obeys Michaelis-Menten kinetics are shown in the table below. The total enzyme concentration is 2.5 nM.