Enzymes and Proteins Flashcards
What are the 2 types of inhibitors
competitive and non-competitive
Outline competitive inhibitors
- bind at the active site of the enzyme
- they have a similar shape to the substrate
- prevent substrate from binding to active site
Solution for competitive inhibitors
increasing the concentration of substrates, decreases the impact of competitive inhibition, as fewer of the inhibitors are able to bind to the active site
What happens to the Vmax for competitive inhibitors
Vmax is not changed as there is still a substrate concentration where full enzyme activity can be achieved
What happens to the Km for competitive inhibitors
The Km is increased as it takes a higher substrate concentration to reach Vmax
Outline non-competitive inhibitors
- bind to the allosteric site of the enzyme
- alter the shape of active site and prevents the substrate to bind to the active site of enzyme
Solution for non-competitive inhibitors
no solution: increasing the concentration of substrates doesn’t reduce the effect of the inhibition
What happens to the Km for non-competitive inhibitors
Km remains unchanged
What happens to the Vmax for non-competitive inhibitors
Vmax decreases
What does Vmax mean/represent
refers to the point where all the active sites are saturated
- a low Vmax = high enzyme activity
- a high Vmax = low enzyme activity
What does Km mean/represent
refers to the substrate concentration which is equal to half of its maximum value
- high Km = high concentration of substrate needed to saturate enzyme (low enzyme-substrate) affinity
Define buffer
substances that resist changes in pH in addition of small amounts of acid or base
What can act as a buffer
amino acids
does an amino acid act as a buffer around its isoelectric point
no
Why can amino acids act as buffers
they can accept and donate protons