Chemical EngineeringA biochemist creates a mutation in the amino acid sequence of
the enzyme acetylcholinesterase (AchE) to research the effect of
this mutation on the enzyme’s catalytic properties. The data
provided below are obtained using 1 nM of each enzyme.
Wild-type AchE: Vmax = 0.06 millimole/min and Km =
10 μM.
Mutant AchE: Vmax = 2 μmole/sec and Km = 1 mM.
WhichQuestion: A biochemist creates a mutation in the amino acid sequence of
the enzyme acetylcholinesterase (AchE) to research the effect of
this mutation on the enzyme’s catalytic properties. The data
provided below are obtained using 1 nM of each enzyme.
Wild-type AchE: Vmax = 0.06 millimole/min and Km =
10 μM.
Mutant AchE: Vmax = 2 μmole/sec and Km = 1 mM.
Which.A biochemist creates a mutation in the amino acid sequence of
the enzyme acetylcholinesterase (AchE) to research the effect of
this mutation on the enzyme’s catalytic properties. The data
provided below are obtained using 1 nM of each enzyme.
Wild-type AchE: Vmax = 0.06 millimole/min and Km =
10 μM.
Mutant AchE: Vmax = 2 μmole/sec and Km = 1 mM.
Which enzyme has the higher affinity for
substrate? Answermutantwild-type
The turnover number of the wild-type enzyme
is Answer s-1and the mutant enzyme
is Answers-1. Round answer to nearest
integer.
Which enzyme has the greater catalytic
efficiency? Answermutantwild-type
Which enzyme shifts the equilibrium further to formation
of products?
mutant OR
neither enzyme because catalysts do not affect equilibria of
reactions OR
wild-type
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