The aminolysis reaction of streptomyces S9 aminopeptidase promotes the synthesis of diverse prolyl dipeptides.
Prolyl dipeptide synthesis by S9 aminopeptidase from Streptomyces thermocyaneoviolaceus (S9AP-St) has been demonstrated. In the synthesis, S9AP-St preferentially used l-Pro-OBzl as the acyl donor, yielding synthesized dipeptides having an l-Pro-Xaa structure. In addition, S9AP-St showed broad specificity toward the acyl acceptor. Furthermore, S9AP-St produced cyclo (l-Pro-l-His) with a conversion ratio of substrate to cyclo (l-Pro-l-His) higher than 40%.
Arima
Jiro
J
Department of Agricultural, Biological, and Environmental Sciences, Faculty of Agriculture, Tottori University, Tottori 680-8553, Japan. arima@muses.tottori-u.ac.jp
Morimoto
Masazumi
M
Usuki
Hirokazu
H
Mori
Nobuhiro
N
Hatanaka
Tadashi
T
D000626:Aminopeptidases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004151:Dipeptides / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004151:Dipeptides; D011994:Recombinant Proteins; D000626:Aminopeptidases