1.4.2 Enzymes Flashcards
What are enzymes?
Enzymes are biological catalysts that increase the rate of reaction by lowering the activation energy of the reaction they catalyse
How do enzymes lower activation energy?
Specific tertiary structure determines shape of active site, complementary to a specific substrate
Formation of enzyme-substrate (ES) complexes lowers activation energy of metabolic reactions
What are enzymes made up of?
Enzymes are 3D tertiary structured globular proteins whose shape is determined by the primary sequence of amino acids
Describe the active site of an enzyme
The active site is an area of the enzyme that is made up of only a few amino acids and forms a small depression in the overall enzyme
Describe the substrate
The substrate is the part of the molecule that the enzyme acts upon
Explain the induced it model of enzyme action
- Shape of active site is not directly complementary to substrate and is flexible
- Conformational change enables ES complexes to form
- This puts strain on substrate bonds, lowering activation energy
How have models of enzyme action changed?
- Initially lock and key model: rigid shape of active site complementary to only 1 substrate
- Currently induced fit model: also explains why binding at allosteric sites can change shape of active site
How could a student identify the activation energy of a metabolic reaction from an energy level diagram?
Difference between free energy of substrate and peak of curve
Name the 5 factors that affect the rate of enzyme-controlled reactions
- Enzyme concentration
- Substrate concentration
- Concentration of inhibitors
- pH
- Temperature
How does substrate concentration affect rate of reaction?
As concentration of substrate increases, rate of reaction increases as more ES complexes are formed
Beyond a certain point, the rate of reaction no longer increases as enzyme concentration becomes the limiting factor
How does enzyme concentration affect rate of reaction?
The rate of reaction increases as enzyme concentration increases as there are more active sites for substrates to bind to
Increasing the enzyme concentration beyond a certain point has no effect on the rate of reaction as there are more active sites than substrates so substrate concentration becomes the limiting factor
How does temperature affect the rate of reaction?
Rate of reaction increases up to the optimum temperature as the kinetic energy of the enzyme increases
Above the optimum temperature rate of reaction decreases beyond the optimum temperature as the enzyme becomes denatured
How does pH affect rate of reaction?
pH affects the enzymes shape as it can disrupt the bonds in the tertiary structure of the enzyme. Like temperature all enzymes work at different optimum pH’s
Describe competitive inhibitors
- Similar shape to substrate = bind to active site
- Don’t stop reaction ; ES complex forms when inhibitor is released
- Increasing substrate concentration decreases their effect
Describe non-competitive inhibitors
- Bind at allosteric binding site
- May permanently stop reaction ; triggers active site to change shape
- Increasing substrate concentration has no impact on their effect