An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.
Pepsin reacts stoicheiometrically with the active-site-directed irreversible inhibitor N-diazoacetyl-l-phenylalanine methyl ester, with concomitant loss of all proteolytic and peptidolytic activity. The reagent esterifies a unique aspartic acid residue in pepsin, which is in the sequence:Ile-Val-Asp-Thr-Gly-Thr-Ser
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000032:analysis*; D001665:Binding Sites; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D004586:Electrophoresis; D004952:Esters; D010434:Pepsin A / Q000032:analysis* / Q000037:antagonists & inhibitors; D010649:Phenylalanine
D004952:Esters; D001224:Aspartic Acid; D010649:Phenylalanine; D010434:Pepsin A