Question

You are working with an enzyme altase that you denature in the presence of urea. If altase were denatured no further by the addition of mercaptoethanol, what would that suggest to you about the enzyme?

Answer 1

If the enzyme altase is denatured by urea but not by mercaptoethanol, it implies disulfide bonds are not essential for the enzyme's structure as mercaptoethanol targets these specific bonds.

Step-by-step explanation:

If altase were denatured by urea but not further denatured by the addition of mercaptoethanol, it suggests that disulfide bonds are not crucial for the enzyme's tertiary or quaternary structure. Urea disrupts hydrogen bonds and other non-covalent interactions, leading to the unfolding of the protein. However, mercaptoethanol specifically breaks disulfide bonds, which are covalent bonds between cysteine residues in a protein. The lack of further denaturation by mercaptoethanol implies that such bonds either do not exist in altase or are not essential for maintaining its active structure.