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Journal of Bacteriology, September 2005, p. 5910-5917, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.5910-5917.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Novel ß-Peptidyl Aminopeptidase (BapA) from Strain 3-2W4 Cleaves Peptide Bonds of Synthetic ß-Tri- and ß-Dipeptides

Birgit Geueke,¹ Kenji Namoto,^2, Dieter Seebach,² and Hans-Peter E. Kohler^1*

Swiss Federal Institute of Environmental Science and Technology (EAWAG), Dübendorf, Switzerland,¹ Laboratory of Organic Chemistry, Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology, Zürich, Switzerland²

Received 11 April 2005/ Accepted 8 June 2005

A novel bacterial strain that was capable of growing on the ß-tripeptide H-ßhVal-ßhAla-ßhLeu-OH as the sole carbon and nitrogen source was isolated from an enrichment culture. On the basis of physiological characterization, partial 16S rRNA sequencing, and fatty acid analysis, strain 3-2W4 was identified as a member of the family Sphingomonadaceae. Growth on the ß-tripeptide and the ß-dipeptide H-ßhAla-ßhLeu-OH was observed, and emerging metabolites were characterized. Small amounts of a persisting metabolite, the N-acetylated ß-dipeptide, were identified in both media. According to dissolved organic carbon measurements, 74 to 80% of the available carbon was dissimilated. The ß-peptide-degrading enzyme was purified from the crude cell extract of cells from strain 3-2W4 grown on complex medium. The enzyme was composed of two subunits, and the N-terminal sequences of both were determined. With this information, it was possible to identify the complete nucleotide sequence and to deduce the primary structure of the gene bapA. The gene encoded a ß-peptidyl aminopeptidase (BapA) of 402 amino acids that was synthesized as preprotein with a signal sequence of 29 amino acids. The enzyme was cleaved into two subunits (residues 30 to 278 and 279 to 402). It belonged to the N-terminal nucleophile (Ntn) hydrolase superfamily.

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* Corresponding author. Mailing address: EAWAG, Überlandstrasse 133, CH-8600 Dübendorf, Switzerland. Phone: 41 1 823 5521. Fax: 41 1 823 5547. E-mail: kohler{at}eawag.ch.

Present address: Novartis Institute of Biomedical Research, Novartis Pharma AG, Basel, Switzerland

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Journal of Bacteriology, September 2005, p. 5910-5917, Vol. 187, No. 17
0021-9193/05/$08.00+0     doi:10.1128/JB.187.17.5910-5917.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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