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Biochemistry

Favouring the unfavoured

Nature volume 483, pages 285–286 (2012)Cite this article

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The naturally occurring antibiotic lasalocid A contains a chemical structure that is not expected to form readily. The enzyme that catalyses the formation of this structure has been identified, and its activity is a revelation. See Letter p.355

Lasalocid A and other polyether antibiotics are widely used to control parasitic infections in farm animals, and to enhance feed efficiency in cattle and other ruminants1. They act by binding and carrying alkali-metal cations and protons across bacterial membranes, thereby interfering with essential ion gradients. The polyethers have also attracted considerable attention from scientists who want to identify the biosynthetic origins of these structurally complex substances and unravel the intricate pathways by which they are assembled2. On page 355 of this issue, Hotta et al.3 report the intriguing mechanism of a step in the biosynthesis of lasalocid A, which they worked out using a combination of synthetic organic chemistry, enzymology, protein structural biology and quantum mechanics. Their findings provide insight into the molecular basis for the products formed by this fascinating class of enzymes.

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Figure 1: Polyether antibiotics.

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  1. David E. Cane is in the Department of Chemistry, Brown University, Providence, Rhode Island 02912-9108, USA.,

    David E. Cane

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  1. David E. Cane
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Correspondence to David E. Cane.

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Cane, D. Favouring the unfavoured. Nature 483, 285–286 (2012). https://doi.org/10.1038/483285a

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