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Novay_Z [31]
3 years ago
9

The pyruvate dehydrogenase is allosterically inhibited by all of the following except?

Biology
2 answers:
marishachu [46]3 years ago
8 0

Answer:

The correct answer is option e) "low acetyl coa / coa-sh ratios".

Explanation:

Allosteric inhibition, also known as negative allosteric modulation, occurs when a ligand decreases one enzyme's affinity to its substrate by binding to a site different from the active site. One classic example of allosteric inhibition takes place in pyruvate dehydrogenase, an enzyme that converts pyruvate into acetyl-CoA by a process called pyruvate decarboxylation. Pyruvate dehydrogenase is inhibited by the end products of the reactions that it catalyzes to regulate its activity. Therefore, a low acetyl coa / coa-sh ratios would not inhibited pyruvate dehydrogenase, on the contrary, a high concentration of acetyl coa would inhibit its activity.

MaRussiya [10]3 years ago
4 0

Answer:

e) low acetyl-CoA/CoA-sh ratios

Explanation:

The enzyme pyruvate dehydrogenase is allosterically inhibited by a high concentration of some of the products of the reaction it catalyzes: NADH and Acetyl-CoA, and ATP (since its a enzyme involved in the cellular respiration, a metabolic process that converts organic molecules into energy/ATP).

So, if you have a low ratio of acetyl-CoA/CoA-sh  it means you have a more of CoA-sh than acetyl-CoA, therefore wouldn't allosterically inhibited the enzyme.

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3. Answer: soil; light

Control variable is the variable that could influence the independent variable, but doesn't want to be observed. Control variable should be made same so it wont influence the result.  In this case, the plant use the same amount of soil. The plant also put in front of a same window, so they should get the same amount of sunlight.


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