3.3: Environmental impacts on Enzyme Function Flashcards
Identify two conditions that affect the structure of an enzyme
pH (can disrupt Hydrogen bond interactions) and high temperatures (low temperatures won’t but just are not as efficient)
How does a change in structure affect the function of an enzyme?
It may not be able to bind to the same substrates anymore
Predict three different possible outcomes when there is a change in structure of an enzyme.
- cant bind to the same substrate
- continues to bind with the same substrate
- decreased ability to catalyze reactions
Identify one example of a protein that is reversible after denaturation.
idk
Identify one example of a protein that is non reversible after denaturation.
albumin-protein in eggs is irreversible after it is cooked
What happens to the pH when the concentration of hydrogen ions increases?
The pH lowers and becomes more acidic.
What happens to the pH when the concentration of hydrogen ions decreases?
The pH increases and becomes more basic
What happens to an enzyme when the pH increases or decreases?
It denatures because each kind of enzyme does best at its pH level.
How does the concentration of reactants affect the reaction rate?
The more reactants, the higher the reaction rate is since there are more chances for the enzyme to collide with a substrate.
How does the concentration of products affect the reaction rate?
The more products, less less room there is for reactants, so the reaction rate decreases as the enzymes are less likely to collide.
What happens to an enzyme when the temperature decrease or increases?
Decreases- works fine, but less likely to collide with reactants so there is a lower reaction rate
Increases- initially increases activation rate because there are more collisions, but the enzyme begins to denature stopping the reactions from occuring
How does a change in temperature affect the molecules in the reaction?
Increase-move quicker, allowing more interactions
Decrease-move slower meaning less interactions and collisions between molecules.
How can researchers overcome competitive inhibitors?
They can try to lower the concentration of the molecules.
What is a noncompetitive inhibitor
Noncompetitive inhibitors bind to allosteric sites so that the enzyme changes shape, causing the substrate to not be able to bind to the enzyme
What is a competitive inhibitor?
A molecule that binds to the active site of an enzyme causing the substrate not to be able to bind. It stops reactions from occuring.
