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Chemical biology

A radical change in enzyme catalysis

Nature volume 540, pages 345–346 (2016)Cite this article

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A method has been devised that allows a ketoreductase enzyme to catalyse reactions other than its natural ones. The key is to excite the enzyme's cofactor using light – an approach that might work for other enzymes. See Letter p.414

Enzymes have several advantages over conventional catalysts for organic synthesis. For example, their ability to perform reactions at room temperature in water makes them suitable for environmentally friendly chemical processes. But many synthetically useful reactions cannot be catalysed by naturally occurring enzymes. The quest to expand nature's enzymatic repertoire of transformations is therefore a crucial area of research. On page 414, Emmanuel et al.1 report a strategy that allows ketoreductase enzymes to perform completely different reactions from the ones that they evolved to catalyse.

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Figure 1: Non-natural reactions catalysed by enzymes.

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Authors and Affiliations

  1. Uwe T. Bornscheuer is in the Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, Greifswald University, 17489 Greifswald, Germany.,

    Uwe T. Bornscheuer

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  1. Uwe T. Bornscheuer
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Correspondence to Uwe T. Bornscheuer.

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Bornscheuer, U. A radical change in enzyme catalysis. Nature 540, 345–346 (2016). https://doi.org/10.1038/540345a

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