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• W2912457485 endingPage "6877" @default.
• W2912457485 startingPage "6864" @default.
• W2912457485 abstract "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." @default.
• W2912457485 created "2019-02-21" @default.
• W2912457485 creator A5024537880 @default.
• W2912457485 creator A5037827364 @default.
• W2912457485 creator A5038639784 @default.
• W2912457485 date "2019-03-12" @default.
• W2912457485 modified "2023-09-30" @default.
• W2912457485 title "Biocatalytic Strategies towards [4+2] Cycloadditions" @default.
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