A transglutaminase homologue as a condensation catalyst in antibiotic assembly lines

Pascal D. Fortin, Christopher T. Walsh () and Nathan A. Magarvey
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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

Nature, 2007, vol. 448, issue 7155, 824-827

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.

Date: 2007
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DOI: 10.1038/nature06068

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