Introduction to enzymes Flashcards
1
Q
What are enzymes (2)
A
- Globular proteins that catalyse reactions of ‘substrates’
- Required for almost all biochemical reactions within cells
2
Q
What do enzymes have (5)
A
- An active site that binds the substrate, prior to the reaction
- High efficiency
- High chemical and stereo-specificity
- pH optima
- Temperature optima
3
Q
What is the mechanism of action of enzymes ()
A
- Enzyme + substrate + ES
- ES → EP
- EP → E + P
4
Q
What is Ks (4)
A
- The dissociation constant of ES
- Ks = [E][S]/[ES]
- Same units as concentration (mM)
- Strong binding = High (ES) and low Ks
5
Q
What happens when a substrate binds to the active site (5)
A
- Substrate converted to product by chemical change
- No covalent bonding between enzyme and substrate
- No covalent bond with enzyme means no chemical change to the enzyme
- Intermolecular forces between enzyme and substrate
- Substrate changes form whilst connected to enzyme then there is a dissociation
6
Q
What happens to the equilibrium position with catalysts (3)
A
- Position (left/right) is not affected by enzyme
- Reduced time to reach equilibrium position with enzyme
- Both forward and backwards reaction rates are increased.
7
Q
What are the classifications of enzymes (6)
A
- Oxidoreductase - oxidation/reduction
- Transferase
- Hydrolases - hydrolysis
- Lyases - Split molecules
- Isomerases
- Ligases - Join molecules
8
Q
What are co-factors (2)
A
- non-proteins that many enzymes require in order to work and allow organisms to regulate enzymatic action.
- Some cofactors are small organic molecules called coenzymes (ATP, Vit B1, Vit C)
9
Q
How can bonds between enzyme and substrate be described
A
Not always covalent - e.g. H-bonds
10
Q
What are electrostatic reactions (3)
A
- Between positive and negative charges.
- Charges can be full (+/-) or partial (d+/ d-).
- Hydrophobic bonds
occur between non-polar regions (e.g. hydrocarbons).