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How do i interpret this graph in terms of Vmax of the amylase enzyme.

This is the graph.
Untitled.jpg179.1KB
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Original post by Core
This is the graph.


I'm not really sure what you're asking but I'm guessing it is this.

Copper inhibits enzyme amylase hence why as starch concentration increases, the rate of reaction with copper is less, compared to that of 'no copper'.
Reply 2
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Core
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Original post by telephone
I'm not really sure what you're asking but I'm guessing it is this.

Copper inhibits enzyme amylase hence why as starch concentration increases, the rate of reaction with copper is less, compared to that of 'no copper'.


the questions asks me how these results show that copper Does Not inhibit, or is not an active site inhibitor.
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Original post by Core
the questions asks me how these results show that copper Does Not inhibit, or is not an active site inhibitor.


Could you post the whole question please?
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DeeWave
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If the inhibition was at the active site, then progressively increasing the starch concentration would continue to increase the rate up to the original level as copper ions would be displaced. The difference would be that the slope would be reduced, but the plateau would (theoretically) be at the same level if enough starch was added.

Because the maximum rate (Vmax, at the plateua) is reduced by copper, it shows that there is less enzyme catalysing the reaction. From 8 concentration units onward the enzyme is saturated in both cases. What is likely to have happened is that the copper has poisoned the enzyme. The copper ions bind to a site/sites on the molecule to change the conformation and therefore active site shape, rendering the enzyme non-functional, as enzyme-substrate complexes are not formed. This is non-competitive inhibition.

HTH :smile:

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