Acid (Asp/Glu) proteases
- Asp-endopeptidase EC.3.4.23.-
- Glu-endopeptidase EC.3.4.23.-
Mechanism These proteases are characterized by a conserved motif known as a catalytic dyad consisting of two aspartic acid residues or one glutamic and one aspartic acid residues. One carboxylate groups of these two acid residues assist in proton transfers from a water molecule that acts as the nucleophile, to attack the peptide bond of the peptide or protein to be cleaved. A well-known example of an aspartate protease is pepsin, which is found in the stomach and plays a crucial role in the digestion of proteins.