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19 Cards in this Set
- Front
- Back
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How can the rate of reaction for enzymes can be measured? |
By measuring how fast the product is made by taking measurements of products made against time, or by measuring how fast the substrate is broken down by measuring the amount of substrate left at different times |
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How does temperature speed up enzyme reactions? |
An increase in temperature leads to an increase in kinetic energy for the enzyme and substrate which leads to more collisions more per second which leads to more enzyme-substrate complexes. Increasing the kinetic energy also means that more of the collisions are successful in making an enzyme-substrate complexes |
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How can temperature negatively affect the enzyme? |
If the temperature becomes to high the enzyme vibrates too much which causes some of the bonds holding the enzyme together in its specific shape to break, meaning that the enzymes unique 3D structure changes and so so does its active site meaning it cant make an enzyme-substrate complex |
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What is the optimum temperature for most enzymes inside the body? |
37 Degrees Centigrade |
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What is the optimum pH for most enzymes in the human body? |
pH 7 |
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What enzyme has an optimum pH of 2? |
Pepsin |
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Where is pepsin found? |
In the stomach where there is stomach acid |
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Why can pH denature an enzyme? |
pH is the amount of H+ ions and OH- ions, both of these ions can affect the ionic bonds that hold together the enzymes unique 3D structure and so if the enzyme is not in the correct pH the H+ or OH- ions can break the bonds, changing the enzymes unique 3D structure and therefore its active site meaning it cant form enzyme-substrate complexes |
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How does concentration of the substrate affect the rate of reaction? |
The higher the concentration of substrate the faster the rate of reaction. |
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Why does changing the concentration of the substrate affect the rate of reaction? |
Increasing the concentration of the substrate means there are more substrate molecules which means more collisions happen meaning that more enzyme-substrate complexes can be formed |
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At what point does changing the concentration of the substrate stop having an affect? |
At the saturation point, this is when there are more substrate molecules than enzymes and as enzymes can only affect one molecule at a time and so increasing the amount of substrate does not mean more enzyme-substrate complexes are formed |
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How does changing the concentration of the enzyme affect the rate of reaction? |
The more enzymes there are in a solution the larger the chance of an enzyme colliding with a substrate which means more enzyme-substrate complexes can be formed |
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How do you interpret graphs for enzymes? |
Look at these examples |
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What are the two types of enzyme inhibitors? |
Competitive and non-competitive inhibitors |
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What shape are competitive inhibitors? |
Competitive inhibitors are a similar shape to the substrate that the enzyme wants to bind to |
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How to competitive inhibitors slow down enzyme action? |
Competitive enzymes try to bind to the active sites of the enzyme which means that the substrate can't, competitive inhibitors are also not broken down by the enzyme so they can stop substrates from binding multiple times |
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How does changing the concentration of competitive inhibitors affect the rate of reaction? |
The higher the concentration of competitive inhibitors the more they can take the place of the substrate on the active site meaning that less enzyme-substrate complexes are formed meaning that the higher the concentration of competitive inhibitors the lower the rate of reaction |
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How do non-competitive inhibitors bond to the enzyme? |
Non-competitive inhibitors bind to a part of the enzyme that isn't the active site |
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How do non-competitive inhibitors affect the rate of reaction? |
When non-competitive inhibitors bond to the enzyme they affect the other bonds in the tertiary structure of the enzyme, which alters its unique 3D structure, making it lose its active site, this means it can't bind with substrates meaning that the enzyme can no longer form enzyme-substrate complexes |
