Biology, asked by abhimanyu4910, 9 months ago

Explain how you determined that Claire had low enzyme production. Use your experimental data to explain how you ruled out active site mutations and abnormal pH.

Answers

Answered by homiehurst
63

Answer:

Claire had a low enzyme production rate because her substrates were binding correctly, which would rule out a mutated active site. We were also able to see that abnormal pH was not the issue, because when we took her data and graphed it, her maximum reaction rate was at pH of 9.1. This was in the optimal range for a well-functioning enzyme. So, the pH and active sites were not the issue.

Note: yall should probably reword this if you ever copy paste so it matches your style of writing <3

Answered by rihuu95
1

Answer:

The correct answer to the question-"Explain how you determined that Claire had low enzyme production. Use your experimental data to explain how you ruled out active site mutations and abnormal pH." is-

]Claire had a low enzyme production rate because her substrates were binding correctly, which would rule out a mutated active site.

Explanation:

Here ,we were also able to see that abnormal pH was not the issue, because when we took her data and graphed it, her maximum reaction rate was at pH of 9.1. Claire had a low enzyme production rate because her substrates were binding correctly, which would rule out a mutated active site.

This was in the optimal range for a well-functioning enzyme. So, the pH and active sites were not the issue.

I suspect that our protein stabilizes the enzyme structure, thus keeping it active at sub optimal pH values.The pH dependence is usually due to the side groups of the amino acids. A change in pH changes the protonation pattern and can, in extreme cases, result in protein denaturation.

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