Format:
Online-Ressource
ISSN:
1521-3765
Content:
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.
In:
volume:25
In:
number:28
In:
year:2019
In:
pages:6864-6877
In:
extent:14
In:
Chemistry - a European journal, Weinheim : Wiley-VCH, 1995-, 25, Heft 28 (2019), 6864-6877 (gesamt 14), 1521-3765
Language:
English
DOI:
10.1002/chem.201805412
URN:
urn:nbn:de:101:1-2022080907462873405335
URL:
https://doi.org/10.1002/chem.201805412
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2022080907462873405335
URL:
https://d-nb.info/1264926944/34
URL:
https://doi.org/10.1002/chem.201805412