2.4 enzyme inhibition COPY Flashcards
How does a competitive inhibitor stop enzyme substrate complexes forming?
Blocking the active site so substrate molecules can not bind
How is a competitive inhibitor able to block the active site?
It has a similar shape to the substrate molecules
What do the competitive inhibitor and substrate molecules have to do?
Compete for the active site
What does a competitive inhibitor do?
Prevents enzyme substrate complexes forming
What is the degree of inhibition dependant on?
The the relative concentrations of substrate and inhibitors
What will happen if there is a high concentration of competitive inhibitors?
- More of the active sites will be taken up (blocked)
- hardly any substrate will get to the enzyme
- lower rate of reaction
What will happen if there is a higher concentration of substrate than competitive inhibitor?
• increased chance of substrate getting to the active site
Are competitive inhibitors usually reversible or non reversible?
Reversible
What does a inhibitor being reversible or irreversible depend on?
The strength of the bonds between enzyme and inhibitor
If the inhibition is irreversible what are the bonds like?
- strong covalent bonds
* hard to remove inhibitor
If the inhibition is reversible what are the bonds like?
- weak hydrogen or weak ionic bonds
* weakness means inhibitor can be removed
Where to non competitive inhibitors bind to?
The enzymes allosteric site
What do non competitive inhibitors binding to the allosteric site cause?
Change in the enzymes tertiary structure
What effect does a change in the enzymes tertiary structure have?
Active sites shape is altered
If the active site of an enzyme changes shape what can no longer happen?
- The enzyme and substrate no longer bind
* enzyme can no longer catalase reactions
State what a Non competitive inhibitor does and the effect it has:
- binds to allosteric site
- changes tertiary structure
- alters shape of active site
- substrate can’t bind
- reactions can’t be catalysed