Journal article
Authors list: Karrer, D; Gand, M; Ruhl, M
Publication year: 2021
Pages: 2191-2199
Journal: ChemCatChem
Volume number: 13
Issue number: 9
ISSN: 1867-3880
eISSN: 1867-3899
Open access status: Hybrid
DOI Link: https://doi.org/10.1002/cctc.202002011
Publisher: Wiley
Abstract:
This study introduces a new type of ene/yne-reductase from Cyclocybe aegerita with a broad substrate scope including aliphatic and aromatic alkenes/alkynes from which aliphatic C8-alkenones, C8-alkenals and aromatic nitroalkenes were the preferred substrates. By comparing alkenes and alkynes, a similar to 2-fold lower conversion towards alkynes was observed. Furthermore, it could be shown that the alkyne reduction proceeds via a slow reduction of the alkyne to the alkene followed by a rapid reduction to the corresponding alkane. An accumulation of the alkene was not observed. Moreover, a regioselective reduction of the double bond in alpha,beta-position of alpha,beta,gamma,delta-unsaturated alkenals took place. This as well as the first biocatalytic reduction of different aliphatic and aromatic alkynes to alkanes underlines the novelty of this biocatalyst. Thus with this study on the new ene-reductase CaeEnR1, a promising substrate scope is disclosed that describes conceivably a broad occurrence of such reactions within the chemical landscape.
Citation Styles
Harvard Citation style: Karrer, D., Gand, M. and Ruhl, M. (2021) Expanding the Biocatalytic Toolbox with a New Type of ene/yne-Reductase from Cyclocybe aegerita, ChemCatChem, 13(9), pp. 2191-2199. https://doi.org/10.1002/cctc.202002011
APA Citation style: Karrer, D., Gand, M., & Ruhl, M. (2021). Expanding the Biocatalytic Toolbox with a New Type of ene/yne-Reductase from Cyclocybe aegerita. ChemCatChem. 13(9), 2191-2199. https://doi.org/10.1002/cctc.202002011