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A transglutaminase homologue as a condensation catalyst in antibiotic assembly lines

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  • Pascal D. Fortin

    (Harvard Medical School, Boston, Massachusetts 02115, USA)

  • Christopher T. Walsh

    (Harvard Medical School, Boston, Massachusetts 02115, USA)

  • Nathan A. Magarvey

    (Harvard Medical School, Boston, Massachusetts 02115, USA)

Abstract

A new line in antibiotics Andrimid is a hybrid nonribosomal peptide-polyketide antibiotic that has been isolated from several different types of bacteria in the past twenty years. It is a nanomolar inhibitor of bacterial acetyl-CoA carboxylase, and inhibiting this enzyme blocks a step in prokaryotic fatty acid biosynthesis. Fortin et al. now show that AdmF, one of the enzymes responsible for the biosynthesis of andrimid, is a transglutaminase-like (TGase-like) enzyme that catalyses the formation of a critical amide bond in the natural product. This is the first time a TGase-like enzyme has been shown to be involved in the biosynthesis of an antibiotic. This work suggests that AdmF or related TGase-like enzymes from other microbes may be used to generate new 'unnatural' antibiotics that are active against drug-resistant bacterial pathogens.

Suggested Citation

  • Pascal D. Fortin & Christopher T. Walsh & Nathan A. Magarvey, 2007. "A transglutaminase homologue as a condensation catalyst in antibiotic assembly lines," Nature, Nature, vol. 448(7155), pages 824-827, August.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7155:d:10.1038_nature06068
    DOI: 10.1038/nature06068
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