Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis |
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Authors: | Kathryn E Bushley Daniel R Ripoll B Gillian Turgeon |
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Affiliation: | (1) Department of Plant Pathology & Plant-Microbe Biology, 334 Plant Science Building, Cornell University, Ithaca, NY 14853, USA;(2) Computational Biology Service Unit, Life Sciences Core Laboratories Center, Cornell University, 621 Frank HT Rhodes Hall, Hoy Road, Ithaca, NY 14853 3801, USA |
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Abstract: | Background Most filamentous ascomycete fungi produce high affinity iron chelators called siderophores, biosynthesized nonribosomally by multimodular adenylating enzymes called nonribosomal peptide synthetases (NRPSs). While genes encoding the majority of NRPSs are intermittently distributed across the fungal kingdom, those encoding ferrichrome synthetase NRPSs, responsible for biosynthesis of ferrichrome siderophores, are conserved, which offers an opportunity to trace their evolution and the genesis of their multimodular domain architecture. Furthermore, since the chemistry of many ferrichromes is known, the biochemical and structural 'rules' guiding NRPS substrate choice can be addressed using protein structural modeling and evolutionary approaches. |
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