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Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium

Freeman, Michael F ; Helf, Maximilian J ; Bhushan, Agneya ; Morinaka, Brandon I ; Piel, Jörn

Nature chemistry, 2017-04, Vol.9 (4), p.387-395 [Periódico revisado por pares]

England: Nature Publishing Group

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  • Título:
    Seven enzymes create extraordinary molecular complexity in an uncultivated bacterium
  • Autor: Freeman, Michael F ; Helf, Maximilian J ; Bhushan, Agneya ; Morinaka, Brandon I ; Piel, Jörn
  • Assuntos: Bacteria ; Rhizobium leguminosarum
  • É parte de: Nature chemistry, 2017-04, Vol.9 (4), p.387-395
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
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  • Descrição: Uncultivated bacteria represent a massive resource of new enzymes and bioactive metabolites, but such bacteria remain functionally enigmatic. Polytheonamides are potent peptide cytotoxins produced by uncultivated bacteria that exist as symbionts in a marine sponge. Outside glycobiology, polytheonamides represent the most heavily post-translationally modified biomolecules that are derived from amino acids. The biosynthesis of polytheonamides involves up to 50 site-specific modifications to create a membrane-spanning β-helical structure. Here, we provide functional evidence that only seven enzymes are necessary for this process. They iteratively catalyse epimerization, methylation and hydroxylation of diverse amino acids. To reconstitute C-methylation, we employed the rarely used heterologous host Rhizobium leguminosarum to invoke the activities of two cobalamin-dependent C-methyltransferases. We observed 44 of the modifications to systematically unravel the biosynthesis of one of the most densely modified and metabolically obscure ribosome-derived molecules found in nature.
  • Editor: England: Nature Publishing Group
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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