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@article{1776763, author = {Schuiten, Eva D. and Badenhorst, Christoffel P. S. and Palm, Gottfried J. and Berndt, Leona and Lammers, Michael and Mičan, Jan and Bednář, David and Damborský, Jiří and Bornscheuer, Uwe T.}, article_location = {WASHINGTON}, article_number = {10}, doi = {http://dx.doi.org/10.1021/acscatal.1c00851}, keywords = {catalytic promiscuity; Corynebacterium; epoxide hydrolase; haloalkane dehalogenase; dual activity}, language = {eng}, issn = {2155-5435}, journal = {ACS Catalysis}, title = {Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12}, url = {https://pubs.acs.org/doi/10.1021/acscatal.1c00851}, volume = {11}, year = {2021} }
TY - JOUR ID - 1776763 AU - Schuiten, Eva D. - Badenhorst, Christoffel P. S. - Palm, Gottfried J. - Berndt, Leona - Lammers, Michael - Mičan, Jan - Bednář, David - Damborský, Jiří - Bornscheuer, Uwe T. PY - 2021 TI - Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12 JF - ACS Catalysis VL - 11 IS - 10 SP - 6113-6120 EP - 6113-6120 PB - AMER CHEMICAL SOC SN - 21555435 KW - catalytic promiscuity KW - Corynebacterium KW - epoxide hydrolase KW - haloalkane dehalogenase KW - dual activity UR - https://pubs.acs.org/doi/10.1021/acscatal.1c00851 N2 - Haloalkane dehalogenases and epoxide hydrolases are phylogenetically related and structurally homologous enzymes that use nucleophilic aspartate residues for an S(N)2 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 mu mol 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. ER -
SCHUITEN, Eva D., Christoffel P. S. BADENHORST, Gottfried J. PALM, Leona BERNDT, Michael LAMMERS, Jan MIČAN, David BEDNÁŘ, Jiří DAMBORSKÝ a Uwe T. BORNSCHEUER. Promiscuous Dehalogenase Activity of the Epoxide Hydrolase CorEH from Corynebacterium sp. C12. \textit{ACS Catalysis}. WASHINGTON: AMER CHEMICAL SOC, 2021, roč.~11, č.~10, s.~6113-6120. ISSN~2155-5435. Dostupné z: https://dx.doi.org/10.1021/acscatal.1c00851.
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