This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Arima, J.
Right arrow Articles by Hatanaka, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Arima, J.
Right arrow Articles by Hatanaka, T.
Agricola
Right arrow Articles by Arima, J.
Right arrow Articles by Hatanaka, T.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, June 2006, p. 4225-4231, Vol. 72, No. 6
0099-2240/06/$08.00+0     doi:10.1128/AEM.00150-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Dipeptide Synthesis by an Aminopeptidase from Streptomyces septatus TH-2 and Its Application to Synthesis of Biologically Active Peptides

Jiro Arima, Yoshiko Uesugi, Misugi Uraji, Masaki Iwabuchi, and Tadashi Hatanaka*

Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, Japan

Received 19 January 2006/ Accepted 12 April 2006

Dipeptide synthesis by aminopeptidase from Streptomyces septatus TH-2 (SSAP) was demonstrated using free amino acid as an acyl donor and aminoacyl methyl ester as an acyl acceptor in 98% methanol (MeOH). SSAP retained its activity after more than 100 h in 98% MeOH, and in the case of phenylalanyl-phenylalanine methyl ester synthesis, the enzyme reaction reached equilibrium when more than 50% of the free phenylalanine was converted to the product. In an investigation of the specificity of SSAP toward acyl donors and acyl acceptors, SSAP showed a broad specificity toward various free amino acids and aminoacyl methyl esters. Furthermore, we applied SSAP to the synthesis of several biologically active peptides, such as aspartyl-phenylalanine, alanyl-tyrosine, and valyl-tyrosine methyl esters.


* Corresponding author. Mailing address: Research Institute for Biological Sciences (RIBS), Okayama, 7549-1 Kibichuo-cho, Kaga-gun, Okayama 716-1241, Japan. Phone: 81-866-56-9452. Fax: 81-866-56-9454. E-mail: hatanaka{at}bio-ribs.com.


Applied and Environmental Microbiology, June 2006, p. 4225-4231, Vol. 72, No. 6
0099-2240/06/$08.00+0     doi:10.1128/AEM.00150-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Steinle, A., Bergander, K., Steinbuchel, A. (2009). Metabolic Engineering of Saccharomyces cerevisiae for Production of Novel Cyanophycins with an Extended Range of Constituent Amino Acids. Appl. Environ. Microbiol. 75: 3437-3446 [Abstract] [Full Text]  
  • Arima, J., Uesugi, Y., Iwabuchi, M., Hatanaka, T. (2006). Change in Substrate Preference of Streptomyces Aminopeptidase through Modification of the Environment around the Substrate Binding Site. Appl. Environ. Microbiol. 72: 7962-7967 [Abstract] [Full Text]