Module 2: Foundations In Biology: Enzymes 🟢 Flashcards
(20 cards)
Active site
- unique-shaped part of an enzyme
- binds to a substrate
Activation energy
The minimum amount of energy required for a reaction to occur
Enzyme-substrate complex
- forms when an enzyme and substrate collide and bind.
- the result is a lowered activation energy
Denature
-when the active site changes shape
- this means the substrate can no longer bind
Enzyme-inhibitor complex
- when an enzyme and inhibitor collide and bind
- prevents the enzyme-substrate complexes from forming
Lock and key hypothesis
- model stating that the enzyme is like a lock and the substrate is a key
- the substrate fits into its enzyme due to the enzymes specific tertiary structure
- they must both be complementary to one another to form an enzyme-substrate complex
Induced fit hypothesis
- the enzyme active site changes shape slightly to accommodate the substrate as it binds
- this puts strain on the substrate weakening the bonds
- lowers the activation energy
Factors affecting enzymes
- temperature
- pH
- enzyme concentration
- substrate concentration
Effect of temperature on rate of reaction
- at low temperatures, there is insufficient kinetic energy for successful collisions
- if the temperature is too high, ionic and hydrogen bonds break, enzymes denature and enzyme substrate complexes cannot form
Q10 temperature coefficient
The Q10 temperature coefficient is measure of the rate of change of an enzyme-controlled reaction as a result of increasing the temperature by 10 degrees
Q10= rate of reaction (x+10) degrees / rate of reaction at x degrees
Effect of substrate concentration on rate of reaction
- if there is low concentration of substrate , the reaction rate will be lower because fewer collisions will occur
- increasing the substrate concentration increases the rate of reaction
- at high substrate concentrations , the rate of reaction will plateau because all of the enzymes active site are saturated
Effect of enzyme concentration on rate of reaction
- at low enzyme concentrations, there will be a lowered activation rate of reaction due to less available enzymes for collisions
- increasing enzyme concentration will increase the rate of reaction as enzyme-substrate complexes are more likely to form
- rate plateaus at high enzyme concentrations due to insufficient availability of substrate
Effect of pH on rate of reaction
- enzymes have a narrow optimum pH range
- outside of the range = denaturation
Non-competitive inhibitors
- bind to the enzyme away from the active site (allosteric site)
- causing the active site to change shape slightly
- enzyme-substrate complexes cannot form
- rate of reaction is much slower
Competitive inhibitors
- competitive inhibitors are a similar shape as the substrate and so, it binds to the active site of the enzyme
- this prevents the substrate from binding
- most competitive inhibitors are reversible
- once the inhibitor is removed, the reaction rate increases
End-product inhibition
• a type of negative feedback where the final product of a metabolic pathway binds to an allosteric site on an enzyme earlier in the pathway.
• This inhibits the enzyme, slowing or stopping the reaction.
• It helps prevent overproduction , saving energy and maintaining balance
- prevents waste
Coenzymes and cofactors
- coenzymes are organic molecules , cofactors are inorganic molecules
- their function is to bind to the active site of an enzyme to make it complementary to the substrate
- the inactivated protein is called an apoenzyme
- when it is activated by the binding of the cofactors, it is called the holoenzyme
Metabolic poison
Substance that damages cells by interfering with metabolic reactions . Usually an inhibitor
How do some medicinal drugs act as inhibitors
Penicillin: non-competitive inhibitor of transpeptidase to prevent formation of peptidoglycan cross-links in bacterial cell wall.
Ritonavir: inhibits HIV protease to prevent assembly of new virions
What is an Enzyme?
An enzyme is a biological catalyst that speeds up the rate of a chemical reaction without being used up, by lowering the activation energy of the reaction.
- usually a globular protein
- It has a specific tertiary structure that determines the shape of its active site, which is complementary to its substrate.