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

Appl Environ Microbiol. 2010 Jun;76(12):4109-12. doi: 10.1128/AEM.00577-10. Epub 2010 Apr 23.

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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminopeptidases / genetics
  • Aminopeptidases / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Dipeptides / chemistry
  • Dipeptides / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Streptomyces / enzymology*
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Dipeptides
  • Recombinant Proteins
  • Aminopeptidases