This enzyme uses its tyrosine-75, glycine-76, and threonine-77 residues to stabilize its substrate, and it can be irreversibly inactivated by diazoacetyl-DL-norleucine.  
This enzyme uses its tyrosine-75, glycine-76, and threonine-77 residues to stabilize its substrate, and it can be irreversibly inactivated by diazoacetyl-DL-norleucine.  It preferentially cleaves at the N-terminal side of aromatic amino acids using an aspartic acid residue in its active site, and its precursor is released from chief cells in response to gastrin. It is activated when it cleaves off 44 of its own amino acids in response to increased acidity. First discovered by Theodore Schwann, FTP, name this enzyme, which is active only in very low pH environments, that cleaves proteins in the stomach during digestion.
This enzyme uses its tyrosine-75, glycine-76, and threonine-77 residues to stabilize its substrate, and it can be irreversibly inactivated by diazoacetyl-DL-norleucine.  
{Pepsin}