Topic 1.5-7 Biological molecules Flashcards
Describe the structure of enzymes
Globular proteins
Specific tertiary structure determines shape of acitve site, complementary to specific substrate
Explain the function of enzymes
Biological catalysts for intra (e.g. DNA polymerase) and extra cellular (e.g. digestive enzymes in tears) reactions.
Formation of enzyme-substrate (ES) complexes lowers activation energy of metabolic reactions.
Explain the lock and key hypothesis
The active site of an enzyme is very specific and only one substrate or type of substrate will fit in it, this is called specificity.
- Random movement causes the enzyme and substrate to collide, the substrate enters the active site
- An enzyme-substrate complex forms. Charged groups attract, distorting the substrate and aiding bond breakage or formation
- Products are released from the active site, leaving the enzyme unchanged and ready to accept another substrate molecule
Explain the induced fit hypothesis
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.
Name five factors that effect the rate of enzyme-controlled rates of reactions
- Enzyme concentration
- Substrate concentration
- Concentration of inhibitors
- pH
- Temperature
How does substrate concentration affect rate of reaction?
Given that the enzyme conc. is fixed, rate increases proportionally to substrate conc..
Rate levels off when maximum number of ES complexes form at any given time.
How does enzyme concentration effect rate of reaction?
Given that the substrate is in excess, rate increases proportionally to enzyme conc..
Rate levels off when maximum number of ES complexes form at any given time.
How does temperature effect rate of reaction in an enzyme controlled reaction?
Rate increases as kinetic energy increases and peaks at optimum temperature.
Above optimum temperature, ionic and hydrogen bonds in 3o structure break = active site no longer complementary to substrate (denaturation).
How does pH affect rate of reaction in an enzyme controlled reaction?
Enzymes have a norrow optimum pH range.
Outside range, H+/OH- ions interact with hydrogen and ionic bonds in 3o structure = denaturation.
How do enzymes lower activation energy?
- By bringing substances close together in the active site so bonds are easier to form
- By putting strain on bonds in the substrate to break them appart
Why do organisms need enzymes?
Without enzymes biochemical reactions happen to slowly at the temperature at which living things can survive
How do competitve inhibitors work?
Bind to active site since they have similar shape to substrate. Temporarily prevent ES complexes from forming until released.
Increasing substrate concentration decreases their effect.
How do non-competitive inhibitors work?
Bind to allosteric site.
Trigger conformational change of active site.
Increasing substrate conc. has no impact on their effect.
What is end product inhibition?
One of the products of a reaction acts as a competitive or non-competitive inhibitor for an enzyme involved in the pathway. Prevents further formation of products.
Why is it advantageous to calculate initial rate?
Represents maximum rate of reaction before conc. of reactants decreases and end-product inhibition.