What amino acid residue present in the specificity pocket allows trypsin to bind to peptides containing arg or lys?

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28-07-2022
Chemistry

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What amino acid residue present in the specificity pocket allows trypsin to bind to peptides containing arg or lys?

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AarushiAanand AarushiAanand · Answer 1 · 2022-08-06T10:06:59+02:00

The amino acid residue present in the specificity pocket allows trypsin to bind to peptides containing arg or lys will be "Asp".

Chymotrypsin breaks down peptide bonds following side chains with a lot of mass or fragrance, like those found in the amino acids phenylalanine as well as tyrosine. The substrate-binding site, also known as the specificity pocket, contains deep and features hydrophobic side chains.

A medium-sized globular protein called trypsin, also known as serine protease 1, serves as a pancreatic serine protease. This enzyme breaks down peptides on the C-terminal portion of the amino acid sequences lysine as well as arginine to hydrolyze bonds.

Therefore, the amino acid residue present in the specificity pocket allows trypsin to bind to peptides containing arg or lys will be "Asp".

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