Question

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Question 17 in the intestines, chymotrypsinogen is activated to form chymotrypsin when trypsin cuts the chymotrypsinogen polypeptide. the lle at position 16 moves to form the substrate binding site. None of the choices is correct All of the choices are correct. the lle at position 16 moves to form the oxyanion hole. Question 18 In a serine protease, the alkoxide ion binds to ATP is an allosteric inhibitor, is the reactive group. determines substrate specificity. stabilizes the tetrahedral intermediate

Answer 1

Ans-17) In the intestine, chymotrypsinogen is activated to form chymotrypsin when (a) trypsin cuts the chymotrypsinogen polypeptide.

Chymotrypsinogen is activated into its active form, chymotrypsin by the enzyme trypsin. This active form is called π-chymotrypsin and is used to create α-chymotrypsin. Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16.

ANS-18) In a serine protease, the alkoxide ion ​​​​​​(c) is the reactive group.

An alkoxide is the conjugate base of an alcohol and therefore consists of an organic group bonded to a negatively charged oxygen atom. They are written as RO−, where R is the organic substituent. Alkoxides are strong bases and, when R is not bulky, good nucleophiles and good ligands.