Metal-ion-assisted hydrolysis of dipeptides involving a serine residue in a neutral aqueous solution

Literature Information

Publication Date 2003-01-23
DOI 10.1039/B209565C
Impact Factor 3.876
Authors

Morio Yashiro, Yoko Sonobe, Ai Yamamura, Tohru Takarada, Makoto Komiyama, Yuki Fujii


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Abstract

Dipeptides having a serine residue at the C-terminus, X-Ser, where X is an appropriate amino acid residue, were efficiently hydrolyzed in the presence of ZnCl2 at pH 7.0. The rapid hydrolysis of X-Ser is due to an autocatalysis of the hydroxy group in the serine residue, and is found to be accelerated by a metal ion, in particular by ZnCl2. Roles of the metal ion in the hydrolysis of peptides involving a serine residue, in relation to the recently reported protein cleavages, are discussed.

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Organic & Biomolecular Chemistry

Organic & Biomolecular Chemistry
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