AH L1 - The Origins of Enzyme Catalytic Rate Enhancement Flashcards
What are enzymes made of and what do they do?
Proteins.
Catalyses nearly all chemical reactions in living organisms.
Are all enzymes made of proteins?
No - catalytic RNA eg hammerhead ribozyme
How much do enzymes accelerate reactions by factors of?
10^6 to 10^7
How have the 3D structures of enzymes been solved ?
X-ray crystallography & cryoelectron microscopy.
Why is it important to study enzymes?
- Essential for cellular function.
- Targets for drug action.
- Used in biotech industries.
What are some enzyme drug targets?
- G - protein-coupled receptors.
- Ligand-gated ion channels
- Voltage-gates ion channels
- Nuclear hormone receptors.
- **Catalytic Receptors
- Kinases
- Proteases**
- Transporters
- Other enzymes
What is this symbol ‡? What does it mean?
Double Dagger.
Preferential stabilization of the transition state.
What is the equation for the non-catalysed reaction?
S <-> P
S= ground state at start = substrate
P = ground state at end = product
What is the formula for an enzyme catalysed reaction?
E + S <-> E.S <-> E.P <-> E + P
What does delta G mean?
the change in free energy
What do enzymes do to ∆G^‡?
It reduces it so that effects the rate at which chemical equilibrium is obtained.
What is ∆G⌄B?
Intrinsic binding energy - refers to the total interaction energy btwn the transition state and enzyme functional groups.
What is a major source of free energy used by enzymes?
Intrinsic binding energy.
What does ∆G⌄B show between the enzyme and transition state?
Favourable interactions i.e. favourable intrinsic binding energy.
What thermodynamic factors does intrinsic binding energy (∆G⌄B) need to overcome?
- Loss of entropy of molecules in solution.
- Desolvation (removal of solvent from a material in solution) on binding of substrate(s).
- Distortion of substrates that occurs in many reactions.
- Alignment of catalytic functional groups on the enzyme.