The aminolysis reaction of streptomyces S9 aminopeptidase promotes the synthesis of diverse prolyl dipeptides.

ABSTRACT: 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%.

SUBMITTER: Arima J 

PROVIDER: S-EPMC2893465 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature