D. Konz et al., Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin, J BACT, 181(1), 1999, pp. 133-140
Lichenysins are surface-active lipopeptides with antibiotic properties prod
uced nonribosomally by several strains of Bacillus licheniformis. Here, we
report the cloning and sequencing of an entire 26.6-kb lichenysin biosynthe
sis operon from B. licheniformis ATCC 10716, Three large open reading frame
s coding for peptide synthetases, designated licA, licB (three modules each
), and licC (one module), could be detected, followed by a gene, licTE, cod
ing for a thioesterase like protein. The domain structure of the seven iden
tified modules, which resembles that of the surfactin synthetases SrfA-A to
-C, showed two epimerization domains attached to the third and sixth modul
es. 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 Gin, Asp, and Ile (with minor Val and Leu substituti
ons), respectively. Therefore, we suppose that the identified biosynthesis
operon is responsible for the production of a lichenysin variant,vith the p
rimary 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.