You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table.   ?maxVmax (μmol min−1) ?MKM (mM) Wild‑type 100 10 Mutant 1 0.1 Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1k−1 is much larger than ?2,k2, which of the following statements are correct?   The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax.   Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. ?0=V0=

Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table.

  ?maxVmax
(μmol min−1)
?MKM
(mM)
Wild‑type 100 10
Mutant 1 0.1
Compare the kinetic parameters of the two versions using the data in the table.
Assuming a two-step reaction scheme in which ?−1k−1 is much larger than ?2,k2, which of the following statements are correct?
 
The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax.
The wild‑type version has a higher affinity for the substrate.
The mutant version has a higher affinity for the substrate.
The mutant version requires a greater concentration of substrate to achieve ?maxVmax.
 
Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM.
?0=V0=
 
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