The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis

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The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.

Glycine residues are known to contribute to conformational flexibility of polypeptide chains, and have been found to contribute to flexibility of some loops associated with enzymic catalysis. A comparison of porcine pepsin in zymogen, mature and inhibited forms revealed that a loop (a flap), consisting of residues 71--80, located near the active site changed its position upon substrate binding....

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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

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2000

ISSN: 0264-6021

DOI: 10.1042/0264-6021:3490169