4.3 Enzyme Inhibitors Flashcards
Why is it important the cellular conditions are kept within narrow limits?
So that enzyme activity is not delayed
Why is it important that reactions to not occur too fast?
Because it could lead to the build-up of excess products
What can enzymes be activated with?
Cofactors
What can enzymes be inactivated with?
Inhibitors
What are inhibitors?
Molecules that prevent enzymes from carrying out their normal function of catalysis
What are the two key types of inhibition?
Competitive and non-competitive.
What happens between competitive inhibitors and substrate molecules?
They compete with each other to bind to the active site of an enzyme.
Are most competitive inhibitors reversible or irreversible?
Reversible.
How does a competitive inhibitor work?
-Inhibitor binds to the active site, competing with the normal substrate
-Substrate is unable to bind to the active site, preventing the reaction.
Describe how a competitive inhibitor changes the rate of reaction, and explain why.
-It reduces the rate of a reaction for a given concentration of a substance, but it does not change the maximum rate of reaction of the enzyme it inhibits.
-If the substrate concentration is enough, there will be so much more substrate than inhibitor that the original maximum rate of reaction can still be reached.
How does a non-competitive inhibitor work? (Simple answer)
It binds to the allosteric site, not the active site
What is the name of the site that the non-competitive inhibitor binds to?
Allosteric site
Describe how a non-competitive inhibitor works (long answer)
-Inhibitor binds to the enzyme at a location that is not the active site
-The binding of the inhibitor causes the tertiary structure of the enzyme to change, meaning the active site changes shape
-This results in the enzyme no longer having a complementary shape to the substrate, so it is unable to bind to the enzyme.
-The enzyme cannot carry out its function, and is inhibited.
Describe how a non-competitive inhibitor changes the rate of reaction, and explain why.
-It decreases the rate of reaction permanently
-Increasing the concentration of enzyme or substrate will not overcome the effect of a non-competitive inhibitor.
Is the binding of a non-competitive inhibitor reversible or irreversible?
Both.