What is the role of enzymes
Biological catalysts
What is the role of catalase
Catalase is an intracellular enzyme. Catalase binds to the toxic chemical hydrogen peroxide and turns it into water + oxygen
What is the role of amylase
Amylase is produced in the pancreas and released into the small intestine. Turn starch into maltose.
Extracellular enzyme
What is the role of trypsin
Produced by the pancreas and released into the digestive system. Breaks down protein molecules into peptides.
Extracellular enzyme
Name 3 features of globular proteins
Hydrophilic amino acids
Hydrophobic amino acids buried in their centre
Soluble in water
How do enzymes increase the RoR?
Enzymes provide a pathway for the reaction with a lower energy barrier.
What is the lock and key model?
Scientists thought the tertiary structure of the active site was fixed and did not change
What is the induced fit?
As the substrate forms bonds with the amino acids in the active site,
the tertiary structure changes to ensure the active site forms perfects to the substrate.
Explain why enzymes are specific to their substrate.
Molecules that are not the substrate can’t form the correct bonds to the amino acids in the active site.
Therefore the tertiary structure of the enzyme does not change, so the shape of the active site does not adjust to fit the model.
What does RoR depend on?
Rate depends on the frequency of successful collisions between the substrate and the active site of the enzyme
Why does the RoR increase as we increase the temperature?
This is because kinetic energy increases for the enzyme and substrate.
Because they are moving more rapidly the frequency of collisions between the substrate and the active site increases.
What is the optimum temperature?
Maximum frequency of collisions
How do enzymes denature when its too hot.
Enzymes are vibrating more rapidly. This causes hydrogen bonds etc to break. Tertiary structure changes. No longer complementary to substrate. Substrate can no longer fit in active site.
Why can’t enzymes renature?
Tertiary structure has changed so much it can’t be reversed
What is a temperature coefficient.
Rate of reaction at X + 10/ Rate of reaction at temperature X
Why is the coefficient usually two?
The rate of an enzyme controlled reaction doubles if we increase by 10 degrees
However above the optimum temperature enzymes denature.
What is a pH affected by?
Concentration of H+ ions
How can an pH affect an enzymes
RoR decreases away from optimum pH
Hydrogen ions can bond with the R groups of the amino acids in the protein
This can form temporary bonds to the substrate, prevents the R groups bond to the substrate.
Hydrogen ions can also bond with the R groups on amino acids in the rest of the enzyme molecules.
This can break the bond holding the tertiary structure in place.
Effect of increasing the substrate concentration irreversible competitive inhibitors.
Some irreversible competitive inhibitors bind permanently to the active site. Increasing the substrate concentration will no increase RoR.
Difference between non-competitive and competitive.
NON-COMPETITIVE INHIBITORS do NOT bind to the active site of an enzyme.
Instead they bind to the allosteric site, which causes the tertiary structure to change so the active site changes
DOES NOT have a similar shape to the substrate
Effect of increasing the substrate concentration on NON competitive inhibitors.
RoR is still reduced by the same amount
Non-competitive inhibitor cause the shape of the active site to change so the substrate molecules still cannot bind successfully.
What is a metabolic pathway?
Series of reactions all catalysed by enzymes.
What is end product inhibition an example of?
Negative feedback
Non-competitive inhibition (takes place on the allosteric site)
What is a cofactor?
a non-protein compound required for the enzyme’s activity to occur
Eg. Chloride ions help amylase catalyse reactions.