Biocatalytic Strategies towards [4+2] Cycloadditions

Benjamin R. Lichman, Sarah E. O'Connor, Hajo Kries*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

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.

Original languageEnglish
Pages (from-to)6864-6877
Number of pages14
JournalChemistry - A European Journal
Volume25
Issue number28
Early online date12 Mar 2019
DOIs
Publication statusPublished - 17 May 2019

Bibliographical note

© 2019 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

Keywords

  • biocatalysis
  • Diels–Alderase
  • enzyme design
  • enzyme mechanism
  • [4+2] cyclase

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