Enzymes
- Created by: quitienbek
- Created on: 21-09-19 18:27
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- Enzymes
- Basic
- Globular proteins
- Complementary to one substrate to form an enzyme-substrate complex
- Lower the activation energy
- Hypothesis
- Induced fit
- Enzyme and substrate not initially complementary
- Enzyme moulds round substrate to form E-S complex
- Distorts bonds in substrate and lowers AE
- Products fall away from active site
- Enzymes reverts back to original shape
- Products fall away from active site
- Distorts bonds in substrate and lowers AE
- Enzyme moulds round substrate to form E-S complex
- Enzyme and substrate not initially complementary
- Lock and key
- Enzyme and substrate are complementary
- Fit like a jigsaw to form E-S complex
- Enzyme remains unchanged and product formed
- Fit like a jigsaw to form E-S complex
- Enzyme and substrate are complementary
- Induced fit
- pH
- H+/OH- are attracted to the charges in polypeptide
- Disrupt hydrogen and ionic bonds that maintain tertiary structure
- H+/OH- are attracted to the charges in polypeptide
- Temperature
- Molecules gain EK so more successful collisions
- Atoms within enzyme also gain energy and vibrate
- Hydrogen bonds that maintain tertiary structure break
- Enzyme dentaured
- Hydrogen bonds that maintain tertiary structure break
- Substrate/enzyme concentration
- If one remains constant, rate will increase up to a point
- Limiting factor
- All enzymes are saturated in a given time
- Not enough substrate to fill all active sites
- Limiting factor
- If one remains constant, rate will increase up to a point
- Inhibitors
- A substance which binds to an enzyme to stop or slow down rate of reaction
- Competitive
- Competes with substrate for active site
- Substrate less likely to bind so fewer E-S complexes in a given time
- Block active site
- Increase rate again by increasing substrate concentration
- Non-competive
- Bind to allosteric site and alter shape of enzyme
- Less enzymes available
- Basic
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