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.

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Chapter1: Biochemistry: An Evolving Science
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BIOCHEMISTRY QUESTION
The initial rate (VO) 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.
[S](μm)
16.0
8.0
4.0
2.0
1.0
v (μMsec ¹)
48.5
32.7
19.8
11.1
5.88
(a) Calculate KM for the enzyme, using the estimated slope (slope = (y2-y1)/(x2-x1)) from a
Lineweaver-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 your
work and don't forget to include units).
(c) A second enzyme (Enzyme2) also obeys Michaelis-Menten kinetics. Its kcat and KM are 800 sec-1
and 5 µM, respectively. Which is the more efficient enzyme? Briefly explain
d) Is Enzyme 1 diffusion limited? Explain.
Transcribed Image Text:BIOCHEMISTRY QUESTION The initial rate (VO) 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. [S](μm) 16.0 8.0 4.0 2.0 1.0 v (μMsec ¹) 48.5 32.7 19.8 11.1 5.88 (a) Calculate KM for the enzyme, using the estimated slope (slope = (y2-y1)/(x2-x1)) from a Lineweaver-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 your work and don't forget to include units). (c) A second enzyme (Enzyme2) also obeys Michaelis-Menten kinetics. Its kcat and KM are 800 sec-1 and 5 µM, respectively. Which is the more efficient enzyme? Briefly explain d) Is Enzyme 1 diffusion limited? Explain.
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