0
Still curious? Ask our experts.
Chat with our AI personalities
Vivi
Rene
JudyCompetitive inhibition involves a molecule binding to the active site of an enzyme, directly competing with the substrate. In non-competitive inhibition, the inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's shape and preventing the substrate from binding.
Add your answer:
Earn +20 pts
What is the type of inhibition of invertase by urea?
Urea inhibits invertase through non-competitive inhibition by binding to the enzyme at a site other than the active site. This binding results in a conformational change in the enzyme that reduces its activity.
What is Difference between uncompetitive and non competitive enzyme inhibition?
Uncompetitive inhibition occurs when the inhibitor binds only to the enzyme-substrate complex, preventing the release of the product. Noncompetitive inhibition occurs when the inhibitor binds to both the enzyme and the enzyme-substrate complex, altering the enzyme's shape and reducing its activity.
Chemical mechanisms that can turn off or reduce an enzyme are?
These chemicals are called competitive inhibitors.
What inhibitor binds into the active site of an enzyme not allowing the subrtate to bind?
This would be a competitive inhibitor. It can be a structural analog of the substrate. This type of inhibition can be out competed by adding more substrate. A competitive inhibitor increases the Km of the enzyme.
How does competitive inhibition affect the value of Vmax in enzyme kinetics?
Competitive inhibition decreases the value of Vmax in enzyme kinetics by reducing the rate at which the enzyme can catalyze a reaction. This is because the inhibitor competes with the substrate for binding to the active site of the enzyme, slowing down the overall reaction rate.
