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Journal of Bacteriology, January 1999, p. 133-140, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Molecular and Biochemical Characterization of the Protein Template Controlling Biosynthesis of the Lipopeptide Lichenysin

Dirk Konz, Sascha Doekel, and Mohamed A. Marahiel*

Philipps-Universität Marburg, Fachbereich Chemie/Biochemie, 35032 Marburg, Germany

Received 26 May 1998/Accepted 30 September 1998

Lichenysins are surface-active lipopeptides with antibiotic properties produced nonribosomally by several strains of Bacillus licheniformis. Here, we report the cloning and sequencing of an entire 26.6-kb lichenysin biosynthesis operon from B. licheniformis ATCC 10716. Three large open reading frames coding for peptide synthetases, designated licA, licB (three modules each), and licC (one module), could be detected, followed by a gene, licTE, coding for a thioesterase-like protein. The domain structure of the seven identified modules, which resembles that of the surfactin synthetases SrfA-A to -C, showed two epimerization domains attached to the third and sixth modules. The substrate specificity of the first, fifth, and seventh recombinant adenylation domains of LicA to -C (cloned and expressed in Escherichia coli) was determined to be Gln, Asp, and Ile (with minor Val and Leu substitutions), respectively. Therefore, we suppose that the identified biosynthesis operon is responsible for the production of a lichenysin variant with the primary amino acid sequence L-Gln-L-Leu-D-Leu-L-Val-L-Asp-D-Leu-L-Ile, with minor Leu and Val substitutions at the seventh position.

* Corresponding author. Mailing address: Philipps-Universität Marburg, Fachbereich Chemie/Biochemie, Hans-Meerwein Str., 35032 Marburg, Germany. Phone: (0) 6421-285722. Fax: (0) 6421-282191. E-mail: Marahiel{at}ps1515.chemie.uni-marburg.de.

Journal of Bacteriology, January 1999, p. 133-140, Vol. 181, No. 1
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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