3. Show how the addition of an uncompetitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. Reaction velocity (Vo)→ Vmax Vmax/2 KM Vmax Substrate concentration [S]->> Intercept = 1/Vo Slope=KM/Vmax =-1/KM 0 Intercept = 1/Vmax 1/[S]
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![8. Show how the addition of an uncompetitive inhibitor would affect the reaction velocity and
double-reciprocal plots shown below.
1
Reaction velocity (Vo)
Vmax
Vmax/2
KM
Substrate concentration [S]
Vmax
1/Vo Slope = KM/Vmax
Intercept = -1/KM
0
Intercept = 1/Vmax
1/[S]](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F321fd000-515a-4cf5-ac03-99096af58e6a%2F697d4dbb-ddc5-4ad2-aa6c-0baeb7b19d8b%2Fr9a9gwi_processed.jpeg&w=3840&q=75)
Enzymes are high molecular weight protein that catalyse biochemical reactions. They contain a active site where the substrate binds to form a short lived enzyme-substrate complex that soon dissociates into product and free enzyme.
Catalytic activity of an enzyme is a measure of how much product is formed or how much substrate is converted into product per minute by the enzyme.
Enzyme inhibition is when a inhibitor bind to the enzyme at the active site or another site, which results in either decrease in enzyme's catalytic activity or enzyme's catalytic activity coming to a complete halt.
Enzyme inhibition can be reversible or irreversible.
Reversible inhibition is when the inhibitor binds reversibly to the enzyme. It can be competitive, un-competative or non-competative.
Irreversible inhibition is when inhibitor binds covalently to the enzyme and ends enzyme catalysis.
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