Enzymes - Inhibition Flashcards
what is an enzyme inhibitor
any substance or molecule that slows down the rate of an enzyme-controlled reaction by affecting the enzyme molecule in some way
what are reversible inhibitors
do not permanently bind to the enzyme, can be removed
what are irreversible inhibitors
permanently bind to the enzyme and cannot easily be removed
what affects whether or not an inhibitor is reversible or irreversible
the strength of the bonds between an enzyme and inhibitor
what will the bonds be for reversible inhibitors
ionic or hydrogen
what will the bonds be for irreversible inhibitors
covalent
what are competitive inhibitors
molecules with a similar shape to the substrate molecules. They compete with substrate molecules to bind to the active site (complementary), blocking it so that no reaction takes place.
what does the level of inhibition depend on for competitive inhibitors
relative concentrations of inhibitor and substrate. If there is a higher concentration of inhibitor, there will be fewer active sites available for the substrate.
what are non-competitive inhibitors and how do they work
molecules that bind to the enzyme away from its active site (in allosteric site) and cause a change in tertiary structure of the protein, causing the active site to change shape so substrate can no longer bind to it.
what happens to reaction rates as a result of non-competitive inhibitors
decrease
what effect will increasing substrate concentration have on non-competitive inhibitors
won’t make a difference to reaction rates as the enzyme activity will still be inhibited