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Plasticity of the Malleobactin Pathway and Its Impact on Siderophore Action in Human Pathogenic Bacteria
Author(s) -
Franke Jakob,
Ishida Keishi,
Hertweck Christian
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201500757
Subject(s) - burkholderia pseudomallei , burkholderia , siderophore , biology , gene cluster , gene , bacteria , pathogenic bacteria , microbiology and biotechnology , computational biology , genetics
The human pathogenic bacteria Burkholderia mallei , Burkholderia pseudomallei , and Burkholderia thailandensis harbor a highly conserved gene cluster coding for the biosynthesis of the long sought‐after malleobactins. Four new, unexpected congeners of the malleobactin family that were isolated and fully characterized in this study feature unusual deviations from the parent, ornibactin‐like architecture. Thus, the malleobactin non‐ribosomal peptide synthetase (NRPS) has a rare flexibility that yields diverse peptide backbones, of which one candidate confers pronounced siderophore activity (EC 50 : 8.4 μ M , CAS assay). These findings not only unveil a highly diverse assembly line but also are an important addition to the knowledgebase of the pathogens’ metabolomes.