Questions Bank | Page 137500

An enzyme is known to contain six Cys residues that form three disulfide bonds (and no other Cys residues).

[Note that six Cys residues could randomly form fifteen possible disulfide bond arrangements]

A researcher performs the following sequence of treatments on a sample of this enzyme:

Simultaneous removal of the mercaptoethanol and the urea (while avoiding formation of any intermolecular disulfide bonds).

They find that the sample obtained from the final treatment has 100% of the activity of the original sample of the enzyme.

Which of the following is the best conclusion from this experiment?

The disulfide bonds have no effect on the activity of the enzyme.

50%

The enzyme must have the right combination of disulfide bonds to be active.

The enzyme does not need to be correctly folded to be active.

The amino acid sequence of the enzyme defines its three-dimensional fold.

50%

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