Issue 4, 2003
From the journal:

Organic & Biomolecular Chemistry

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

Morio Yashiro,*a   Yoko Sonobe,b   Ai Yamamura,b   Tohru Takarada,b   Makoto Komiyamab  and  Yuki Fujiic  

* Corresponding authors

a Department of Applied Chemistry, Faculty of Engineering, Tokyo Institute of Polytechnics, 1583 Iiyama, Atsugi, Kanagawa 243-0297, Japan
E-mail: yashiro@chem.t-kougei.ac.jp
Fax: +81 (0)46-242-9554
Tel: +81 (0)46-242-9554

b Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Tokyo 113-8656, Japan

c Department of Chemistry, Faculty of Science, Ibaraki University, Bunkyo 2-1-1, Japan

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.

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

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Article information

DOI
https://doi.org/10.1039/B209565C
Article type
Paper
Submitted
02 Oct 2002
Accepted
20 Dec 2002
First published
23 Jan 2003

Org. Biomol. Chem., 2003,1, 629-632

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

M. Yashiro, Y. Sonobe, A. Yamamura, T. Takarada, M. Komiyama and Y. Fujii, Org. Biomol. Chem., 2003, 1, 629 DOI: 10.1039/B209565C

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