Answer:
The options
A) It is probably an enzyme that is regulated by noncompetitive inhibition.
B) It is probably a multi-subunit enzyme that is regulated by allosteric regulation.
C) It is probably an enzyme that is regulated by competitive inhibition.
D) It is probably an enzyme that is regulated by cooperativity.
The CORRECT ANSWER IS A)
A) It is probably an enzyme that is regulated by noncompetitive inhibition.
Explanation:
This kind of protein is an enzyme that possesses a singular polypeptide chain, that is to say, it lacks more subunits. The pocket is localised in the binding site for the necessary substrate or active site, and the cavity is a binding site for a different molecule. This seperate molecule is a known to be a regulatory molecule or an inhibitor. In this case study, the inhibitor adhere itself to a different site which isn't the active site. When an inhibitor attaches itself in a site which is not the active site, it is reported that this molecule behaves in the form of a noncompetitive inhibitor.
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so He would like to write about the
</span><span>the beauty of a weeping willow
</span>so i conclude option C is correct
hope it helps
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Answer:
The correct answer is - option D. adrenergic receptor.
Explanation:
Adrenergic receptors are present on or in the effector cells that are specific molecular structures. The adrenergic receptors are glycoproteins that are present on the cell surface that binds and recognize with the various hormones or drugs such as norepinephrine or epinephrine and others.
These are the receptors that are sympathetic tissue receptors that get drugs or hormones released from the sympathetic nerve endings and the adrenal glands.
Thus, the correct answer is - option D. adrenergic receptors.
