| Autor: |
Vinnik, Vladimir, Zhang, Fan, Park, Hyunjun, Cook, Taylor B., Throckmorton, Kurt, Pfleger, Brian F., Bugni, Tim S., Thomas, Michael G. |
| Zdroj: |
ACS Chemical Biology; January 2021, Vol. 16 Issue: 1 p125-135, 11p |
| Abstrakt: |
Siderophores are iron-chelating molecules produced by microorganisms and plants to acquire exogenous iron. Siderophore biosynthetic enzymology often produces elaborate and unique molecules through unusual reactions to enable specific recognition by the producing organisms. Herein, we report the structure of two siderophore analogs from Agrobacterium fabrumstrain C58, which we named fabrubactin (FBN) A and FBN B. Additionally, we characterized the substrate specificities of the NRPS and PKS components. The structures suggest unique Favorskii-like rearrangements of the molecular backbone that we propose are catalyzed by the flavin-dependent monooxygenase, FbnE. FBN A and B contain a 1,1-dimethyl-3-amino-1,2,3,4-tetrahydro-7,8-dihydroxy-quinolin (Dmaq) moiety previously seen only in the anachelin cyanobacterial siderophores. We provide evidence that Dmaq is derived from l-DOPA and propose a mechanism for the formation of the mature Dmaq moiety. Our bioinformatic analyses suggest that FBN A and B and the anachelins belong to a large and diverse siderophore family widespread throughout the Rhizobium/Agrobacteriumgroup, α-proteobacteria, and cyanobacteria. |
| Databáze: |
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