Metal-ion-assisted hydrolysis of dipeptides involving a serine residue in a neutral aqueous solution.
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.
Yashiro
Morio
M
Department of Applied Chemistry, Faculty of Engineering, Tokyo Institute of Polytechnics, 1583 Iiyama, Atsugi, Kanagawa 243-0297, Japan. yashiro@chem.t-kougei.ac.jp
Sonobe
Yoko
Y
Yamamura
Ai
A
Takarada
Tohru
T
Komiyama
Makoto
M
Fujii
Yuki
Y
D002712:Chlorides / Q000737:chemistry; D004151:Dipeptides / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D008670:Metals / Q000737:chemistry*; D012694:Serine / Q000737:chemistry*; D012996:Solutions; D017967:Zinc Compounds / Q000737:chemistry
D002712:Chlorides; D004151:Dipeptides; D008670:Metals; D012996:Solutions; D017967:Zinc Compounds; D012694:Serine; C016837:zinc chloride