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Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12
- Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an SN2 attack on their substrates. Despite their mechanistic similarities, no enzymes are known that exhibit both epoxide hydrolase and dehalogenase activity. We screened a subset of epoxide hydrolases, closely related to dehalogenases, for dehalogenase activity and found that the epoxide hydrolase CorEH from Corynebacterium sp. C12 exhibits promiscuous dehalogenase activity. Compared to the hydrolysis of epoxides like cyclohexene oxide (1.41 μmol min–1 mg–1), the dehalogenation of haloalkanes like 1-bromobutane (0.25 nmol min–1 mg–1) is about 5000-fold lower. In addition to the activity with 1-bromobutane, dehalogenase activity was detected with other substrates like 1-bromohexane, 1,2-dibromoethane, 1-iodobutane, and 1-iodohexane. This study shows that dual epoxide hydrolase and dehalogenase activity can be present in one naturally occurring protein scaffold.
Author: | Prof. Dr. Uwe BornscheuerORCiD, Eva D. Schuiten, Christoffel P.S. Badenhorst, Gottfried J. Palm, Leona Berndt, Michael Lammers, Jan Mican, David Bednar, Jiri Damborsky |
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URN: | urn:nbn:de:gbv:9-opus-60335 |
DOI: | https://doi.org/10.1021/acscatal.1c00851 |
ISSN: | 2155-5435 |
Parent Title (English): | ACS Catalysis |
Publisher: | ACS Publications |
Place of publication: | Washington, DC |
Document Type: | Article |
Language: | English |
Year of Completion: | 2021 |
Release Date: | 2022/03/16 |
Tag: | Biokatalyse |
GND Keyword: | Enzym |
Volume: | 11 |
Issue: | 10 |
First Page: | 6113 |
Last Page: | 6120 |
Faculties: | Mathematisch-Naturwissenschaftliche Fakultät |
DDC class: | 500 Naturwissenschaften und Mathematik / 540 Chemie |
Licence (German): | Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung |