Metal-ion-assisted hydrolysis of dipeptides involving a serine residue in a neutral aqueous solutionElectronic supplementary information (ESI) available: Kinetic studies involving pH and concentration profiles of the rate constant. See http://www.rsc.org/suppdata/ob/b2/b209565c/

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.