Biocatalytic Strategies towards [4+2] Cycloadditions |
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Authors: | Dr Benjamin R Lichman Prof Dr Sarah E O'Connor Dr Hajo Kries |
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Institution: | 1. Department of Biological Chemistry, The John Innes Centre, Colney Lane, Norwich, UK;2. Independent Junior Research Group, Biosynthetic Design of Natural Products, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knöll Institute (HKI Jena), Beutenbergstr. 11a, 07745 Jena, Germany |
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Abstract: | Long sought after 4+2] cyclases have sprouted up in numerous biosynthetic pathways in recent years, raising hopes for biocatalytic solutions to cycloaddition catalysis, an important problem in chemical synthesis. In a few cases, detailed pictures of the inner workings of these catalysts have emerged, but intense efforts to gain deeper understanding are underway by means of crystallography and computational modelling. This Minireview aims to shed light on the catalytic strategies that this highly diverse family of enzymes employs to accelerate and direct the course of 4+2] cycloadditions with reference to small-molecule catalysts and designer enzymes. These catalytic strategies include oxidative or reductive triggers and lid-like movements of enzyme domains. A precise understanding of natural cycloaddition catalysts will be instrumental for customizing them for various synthetic applications. |
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Keywords: | [4+2] cyclase biocatalysis Diels–Alderase enzyme design enzyme mechanism |
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