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 Previous Article

Applied and Environmental Microbiology, December 2006, p. 7962-7967, Vol. 72, No. 12
0099-2240/06/$08.00+0     doi:10.1128/AEM.01460-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Change in Substrate Preference of Streptomyces Aminopeptidase through Modification of the Environment around the Substrate Binding Site{triangledown}

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

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

Received 26 June 2006/ Accepted 30 September 2006

We attempted to alter the substrate preference of aminopeptidase from Streptomyces septatus TH-2 (SSAP). Because Asp198 and Phe221 of SSAP are located in the substrate binding site, we screened 2,000 mutant enzymes with D198X/F221X mutations. By carrying out this examination, we obtained two enzymes; one specifically hydrolyzed an arginyl derivative, and the other specifically hydrolyzed a cystinyl derivative (65- and 12.5-fold higher kcat values for hydrolysis of p-nitroanilide derivatives than those of the wild type, respectively).

* 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.

{triangledown} Published ahead of print on 6 October 2006.

Applied and Environmental Microbiology, December 2006, p. 7962-7967, Vol. 72, No. 12
0099-2240/06/$08.00+0     doi:10.1128/AEM.01460-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Arima, J., Uesugi, Y., Iwabuchi, M., Hatanaka, T. (2008). Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain. Protein Eng Des Sel 21: 45-53 [Abstract] [Full Text]  


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