Question

4. Chymotrypsin is an enzyme known to have broad substrate specificity in vivo. Why is it advantageous for chymotrypsin to have broad substrate specificity whereas in the case of other proteases such broad substrate specificity would be viewed as problematic

Answer 1

Answer:

Broad substrate specificity of chymotrypsin would be very dangerous for a protease that plays a role and perform its activities outside of the digestive system.

Explanation:

Chymotrypsin is one of the serine base proteases that includes 3 polypeptide chains. Disulfide bonds held all three polypeptide chains together. Chymotrypsin is a digestive enzyme released by the pancreas into the duodenum.

As a digestive enzyme, chymotrypsin's role is to indiscriminately degrade a large range of proteins that are taken in so that their component AAs can be recovered.

Broad substrate specificity of chymotrypsin would be very dangerous for a protease that plays a role and perform its activities outside of the digestive system.