3.4.23.1 curcumin + H2O i.e. diferuloylmethane 3.4.23.1 additional information the cleavage site of isoform PG1 to produce pepsin is clearly at the 41-42 bond of Phe-Ala 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A1 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. Pepsin A2 does not prefer some hydrophobic residues such as Leu, Val, Ala and Met 3.4.23.1 additional information the enzyme prefers both hydrophobic/aromatic residues and charged residues at the P'1 sites of substrates. The enzyme prefers some hydrophobic residues such as Leu, Val, Ala and Met 3.4.23.1 Proteins + H2O low specificity 3.4.23.1 Proteins + H2O enzyme formed from pepsinogen A, agent of gastric digestion in mammals and birds 3.4.23.1 Proteins + H2O preferential cleavage: Phe-, Leu- 3.4.23.1 trypsinogen + H2O -