Enzyme Properties
- Created by: Ellie Rivers
- Created on: 11-04-13 11:37
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- Enzyme Properties
- Non-competitive Inhibitors
- the inhibitor alters the shape of the enzymes active site so substrates no longer fit
- this means the enzyme can no longer function
- attach themselves to the enzyme at a site which is not the active site
- Effect of Temperature
- the enzyme and substrate molecules come together more frequently
- the molecules move around more rapidly and collide with each other
- a rise in temperature causes a rise in KINETIC ENERGY
- shown as a rising curve on a graph
- the rise in temperature also causes bonds to break, changing the shape of the active site
- at 60 degrees the enzymes are denatured
- Competitive Inhibitors
- they compete with the substrate for available active sites
- they have a molecular shape that is similar to the substrate
- bind to the active site of the enzyme
- if substrate concentration increases, the effect of the inhibitor is reduced
- Effect of pH
- a change in pH can cause the bonds to break and change the enzymes shape
- if the substrate no longer fits the enzyme has been denatured
- a change in pH alters the charge of the active site so the enzyme-substrate complex cannot be formed
- small changes in the pH change the active site
- each enzyme has an optimum pH which it works the fastest
- Effect of Substrate Concentration
- as more substrate is added, more active sites are filled
- at low substrate levels there are a limited amount of substrate molecules to collide
- the rate of reaction is at its optimum when all the active sites are working as fast as they can
- if substrate increases the rate of reaction increases
- Non-competitive Inhibitors
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