Recall that proline often introduces kinks in the backbone of a polypeptide. These kinks make it difficult for enzymes in your gut to fully digest gluten. In people with celiac disease, certain proline-rich peptides left over after gluten digestion will trigger an abnormal immune response. Researchers have identified a mold enzyme called AN-PEP that effectively digests proline-rich peptides. Predict where the structural differences would occur between AN-PEP and other enzymes that do not digest the peptides. A. Amino acid differences would be expected in regions that affect the folded structure of the active site.
B. Amino acid differences would not be expected. The effectiveness of digestion depends on other conditions
C. Amino acid differences would be expected in the site where it binds to bacterial cells or viruses.
D. Amino acid differences would be expected in the active site.

A. Amino acid differences would be expected in regions that affect the folded structure of the active site.

D. Amino acid differences would be expected in the active site.

Explanation:

Gluten is composed of glutenin and gliadin proteins. In celiac disease, the gliadins are not efficiently digested in the gastrointestinal system, thereby long protein fragments reach to the small intestine. The AN-PEP (aspergillus niger-derived prolyl endoprotease) is a digestive enzyme capable of degrading gluten into small protein fragments. However, it is believed that the AN-PEP enzyme is not intended to prevent celiac disease. Proline is an amino acid residue that has a singular cyclic structure, which promotes protein folding, although this structure also alters the peptide bond formation in the ribosome.

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