book 1 (enzyme inhibitors) Flashcards
1
Q
describe how competitive inhibitors work.
A
- competitive inhibitors have similar 3D conformation to substrates
- it competes with substrate for binding to the active site of enzymes
- thus decreasing frequency of effective collisions between enzymes and substrates molecules
- decreases the concentration of enzyme-substate complexes formed per unit time
- decreases the concentration of products formed per unit time
- rate of reaction decreases
2
Q
state the effect of substrate concentration on rate of reaction (competitive inhibitors)
A
1 the increase in substrate concentration increases the frequency of effective collisions between enzyme and substrates as compared to enzyme and inhibitors
- this increases the formation of enzyme-substrate complexes compared to enzyme-inhibitor complexes
- there will be increase in concentration of products formed per unit time
- rate of reaction can still reach the maximum value at high substrate concentration
3
Q
describe how non-competitive inhibitors work
A
- non-competitive inhibitors don’t have similar 3D conformation to the original substrates of enzymes
- thus inhibitor binds to enzyme at a specific region other than the active site
- this changes the 3D conformation of enzyme and alters the 3D conformation of active site
- substrate no longer able to bind to enzyme active site
- this decreases the frequency of effective collisions between enzymes and substrate molecules, thus decreasing the concentration of enzyme-substrate complexes formed per unit time, and decreases the concentration of products formed per unit time
- thus decreasing rate of reactions
4
Q
state the effect of substrate concentration on the rate of reaction (non-competitive)
A
- the increase in the substrate concentration cannot increase rate of reaction as the presence of non-competitive inhibitor renders a proportion of the enzyme molecule out of action
- decreasing the effective enzyme concentration in the reaction mixture
- rate of reaction cannot reach maximum value even at high substrate concentrations
5
Q
describe how allosteric inhibitors work
A
- no similarity in 3D conformation to the original substrate of enzyme
- allosteric inhibitors binds to one of the several allosteric sites on enzymes, altering the 3D conformation of active sites on that subunit and other subunits too
- substrate unable to bind to the enzyme active sites
- this decreases the frequency of effective collisions between enzymes and substrates, decreasing the concentration of enzyme-substrate complexes formed per unit time
- decrease in concentration of products formed per unit time