The first cleavage site in pepsinogen activation.
By incubation of porcine, bovine, canine, or chicken pepsinogens and calf prochymosin with pepstatin at pH 2.5, the first active protein generated on activation is trapped in an inactive complex. The first activation peptide liberated from porcine pepsinogen has been identified as residues 1-16 whereas that from prochymosin is derived from residues 1-27. This suggests that pepsin and chymosin are not formed by one-step conversions from their zymogens, but by (different) sequential, activation mechanisms.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D010435:Pepsinogens / Q000302:isolation & purification / Q000378:metabolism*; D010436:Pepstatins; D010447:Peptide Hydrolases / Q000302:isolation & purification; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013270:Stomach / Q000201:enzymology; D013552:Swine
D000596:Amino Acids; D002241:Carbohydrates; D010435:Pepsinogens; D010436:Pepstatins; D010447:Peptide Hydrolases