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Applied and Environmental Microbiology, January 2006, p. 968-971, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.968-971.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of a Novel PepF-Like Oligopeptidase Secreted by Bacillus amyloliquefaciens 23-7A{dagger}

Shiou-Huei Chao,1 Tzu-Hao Cheng,1 Chin-Ying Shaw,1 Meng-Hwan Lee,1 Yuan-Hsun Hsu,2 and Ying-Chieh Tsai1*

Institute of Biochemistry, National Yang-Ming University,1 Graduate Institute of Medical Science, Taipei Medical University, Taipei, Taiwan2

Received 19 April 2005/ Accepted 6 October 2005

An oligopeptidase from Bacillus amyloliquefaciens 23-7A was characterized along with its biochemical activities and structural gene. The protein's amino acid sequence and enzymatic activities were similar to those of other bacterial PepFs, which belong to metallopeptidase family M3. While most bacterial PepFs are cytoplasmic endopeptidases, the identified PepFBa oligopeptidase is a secreted protein and may facilitate the process of sporulation.

* Corresponding author. Mailing address: Institute of Biochemistry, National Yang-Ming University, 155, Sec. 2, Li-Nong Street, Pei-Tou, Taipei 11221, Taiwan. Phone: (886) 2-2826-7125. Fax: (886) 2-2826-4843. E-mail: tsaiyc{at}ym.edu.tw

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, January 2006, p. 968-971, Vol. 72, No. 1
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.1.968-971.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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