Další formáty:
BibTeX
LaTeX
RIS
@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.
|
