An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide

作者：Richard Bayliss, J.R. Knowles, Grith B. Wybrandt · 发表于：Biochemical Journal · 年份：1969 · DOI：10.1042/bj1130377 · 被引用次数：95 · 研究领域：Carbohydrate Chemistry and Synthesis、Chemical Synthesis and Analysis、Biochemical and Structural Characterization

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