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2 Two version of the same enzyme were isolated, a wild type and a mutant differing at a single amino acid. After a thorough study the following kinetic parameters were accurately measured. For the second blank, use a number with two significant figures. Wild-type Mutant Maximum velocity 90 micromol/min 1 micromol/min Km 10 mM 0.1 mM Assuming a two-step reaction where k-1 is much larger than k2, the choose your answer. form has the higher affinity for the substrate. The initial velocity of the reaction catalyzed by the wild-type enzyme at a substate concentration of 10 mM is type your answer.. micromol/min. choose your answer. enzyme alters the equilibrium more in the direction of the product.

2 Two version of the same enzyme were isolated, a wild type and a mutant differing at a single amino acid. After a thorough study the following kinetic parameters were accurately measured. For the second blank, use a number with two significant figures. Wild-type Mutant Maximum velocity 90 micromol/min 1 micromol/min Km 10 mM 0.1 mM Assuming a two-step reaction where k-1 is much larger than k2, the choose your answer. form has the higher affinity for the substrate. The initial velocity of the reaction catalyzed by the wild-type enzyme at a substate concentration of 10 mM is type your answer.. micromol/min. choose your answer. enzyme alters the equilibrium more in the direction of the product.

Biochemistry
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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2 Two version of the same enzyme were isolated, a wild type and a mutant differing at a single amino acid. After a thorough study the following kinetic parameters were accurately measured. For the second blank, use a number with two significant figures. Wild-type Mutant Maximum velocity 90 micromol/min 1 micromol/min Km 10 mM 0.1 mM Assuming a two-step reaction where k-1 is much larger than k2, the choose your answer... form has the higher affinity for the substrate. The initial velocity of the reaction catalyzed by the wild-type enzyme at a substate concentration of 10 mM is type your answer... micromol/min. choose your answer... enzyme alters the equilibrium more in the direction of the product.
Transcribed Image Text:2 Two version of the same enzyme were isolated, a wild type and a mutant differing at a single amino acid. After a thorough study the following kinetic parameters were accurately measured. For the second blank, use a number with two significant figures. Wild-type Mutant Maximum velocity 90 micromol/min 1 micromol/min Km 10 mM 0.1 mM Assuming a two-step reaction where k-1 is much larger than k2, the choose your answer... form has the higher affinity for the substrate. The initial velocity of the reaction catalyzed by the wild-type enzyme at a substate concentration of 10 mM is type your answer... micromol/min. choose your answer... enzyme alters the equilibrium more in the direction of the product.
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