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

Applied and Environmental Microbiology
Jiro ArimaTadashi Hatanaka

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%.

References

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Citations

May 26, 2010·Applied Microbiology and Biotechnology·Jiro ArimaTadanori Aimi
Jan 6, 2011·Applied Biochemistry and Biotechnology·Tadashi HatanakaYuya Kumagai
Sep 29, 2011·Applied and Environmental Microbiology·Jiro ArimaNobuhiro Mori

Related Concepts

Aminopeptidase
Bacterial Proteins
Dipeptides
Proteins, Recombinant DNA
Streptomyces
Substrate Specificity
Aminopeptidase
Arginine
Dipeptides
Cyclo 3

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