Show how the addition of a competitive inhibitor would affect the reaction velocity and double-reciprocal plots shown below. 1 Reaction velocity (Vo) Vmax Vmax/2 max KM Substrate concentration [S]->> 1/Vo Slope=KM/Vmax Intercept = -1/KM 0 Intercept = 1/Vmax 1/[S]
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![8. Show how the addition of a competitive inhibitor would affect the reaction velocity and
double-reciprocal plots shown below.
1
Reaction velocity (V)
Vmax
Vmax/2
- KM
Vmax
Substrate concentration [S] -
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%2F03c31203-e2fe-4060-8eca-920c3daffcc1%2Fnuuhrf_processed.jpeg&w=3840&q=75)
Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an active site where the substrate binds to form a short-lived enzyme-substrate complex that soon dissociates into a product and free enzyme.
The catalytic activity of an enzyme is a measure of how much product is formed or how much substrate is converted into a product per minute by the enzyme.
Enzyme inhibition is when an inhibitor bind to the enzyme at the active site or another site, which results in either decrease in the enzyme's catalytic activity or the 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-competitive or non-competitive.
Irreversible inhibition is when the inhibitor binds covalently to the enzyme and ends enzyme catalysis.
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