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. 1971 Jun;123(1):75-82.
doi: 10.1042/bj1230075.

An active site peptide from pepsin C

J Kay, A P Ryle

An active site peptide from pepsin C

J Kay et al. Biochem J. 1971 Jun.

Abstract

Porcine pepsin C is inactivated rapidly and irreversibly by diazoacetyl-dl-norleucine methyl ester in the presence of cupric ions at pH values above 4.5. The inactivation is specific in that complete inactivation accompanies the incorporation of 1mol of inhibitor residue/mol of enzyme and evidence has been obtained to suggest that the reaction occurs with an active site residue. The site of reaction is the beta-carboxyl group of an aspartic acid residue in the sequence Ile-Val-Asp-Thr. This sequence is identical with the active-site sequence in pepsin and the significance of this in terms of the different activities of the two enzymes is discussed.

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