The active site of chymotrypsin is made up of Choose one:
O Asp 102 and His57 from the A chain and Ser 195 from the C chain.
O Asp 102 and Ser195 from the B chain and His57 from the C chain.
O Asp 102 and His57 from the A chain and Ser195 from the B chain.
O Asp 102 and His57 from the B chain and Ser195 from the C chain.

Question

12-12-2022
Chemistry

Answered

The active site of chymotrypsin is made up of Choose one:
O Asp 102 and His57 from the A chain and Ser 195 from the C chain.
O Asp 102 and Ser195 from the B chain and His57 from the C chain.
O Asp 102 and His57 from the A chain and Ser195 from the B chain.
O Asp 102 and His57 from the B chain and Ser195 from the C chain.

Answer :

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fawadmohd fawadmohd · Answer 1 · 2022-12-18T02:54:45-05:00

Enzyme Active Sites and their Reaction Mechanisms, Harry Morrison, 2021 α - The "hydrolytic enzyme" chymotrypsin (EC 3.4.21.1; chymotrypsinogen .

A) belongs to the superfamily of serine proteases and hydrolyzes peptide bonds by using a serine hydroxyl group as a nucleophile in the active site. The pancreas is where chymotrypsin is largely made. To stop its protease activity from dissolving the pancreas, it is created as the inactive zymogen chymotrypsinogen rather than the active version. A different enzyme known as trypsin changes it into its active form when it is secreted into the lumen of the small intestine.

Trypsin is the primary enzyme that breaks down chymotrypsin, which is also known as chymotrypsinogen. Active enzymes can occasionally even cleave the incoming inactive form of themselves.

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