How do serine proteases hydrolyze dietary proteins? Describe the catalytic activity of chymotrypsin.

How do serine proteases hydrolyze dietary proteins? Describe the catalytic activity of chymotrypsin.

Expert Solution

queen_honey_blossom answered 1 year ago

Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at...

Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at the C-terminal end of specific residues. Chymotrypsin recognizes aromatic residues, while trypsin recognizes lysine and arginine. The recognition of a particular side chain (side chain specificity) is fully determined by the structure and properties of the binding pocket. In the case of chymotyipsin the binding pocket is hydrophobic and is wide enough to accommodate an aromatic ring. Given what you know about the properties...

Serine proteases...... A) use an Asp, Lys, Ser catalytic triad B) use a Shiff base-enzyme intermediate...

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