| LIŠKOVÁ, Veronika, Veronika ŠTĚPÁNKOVÁ, David BEDNÁŘ, Jan BREZOVSKÝ, Zbyněk PROKOP, Radka CHALOUPKOVÁ a Jiří DAMBORSKÝ. Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites. Online. Angewandte Chemie International Edition. WEINHEIM, GERMANY: WILEY-V C H VERLAG, 2017, roč. 56, č. 17, s. 4719-4723. ISSN 1433-7851. Dostupné z: https://dx.doi.org/10.1002/anie.201611193. [citováno 2024-04-24] |
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@article{1403848,
author = {Lišková, Veronika and Štěpánková, Veronika and Bednář, David and Brezovský, Jan and Prokop, Zbyněk and Chaloupková, Radka and Damborský, Jiří},
article_location = {WEINHEIM, GERMANY},
article_number = {17},
doi = {http://dx.doi.org/10.1002/anie.201611193},
keywords = {enantioselectivity; enzyme catalysis; enzymes; molecular modeling; protein engineering},
language = {eng},
issn = {1433-7851},
journal = {Angewandte Chemie International Edition},
title = {Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites},
url = {https://loschmidt.chemi.muni.cz/peg/publications/different-structural-origins-of-the-enantioselectivity-of-haloalkane-dehalogenases-toward-linear-%CE%B2-haloalkanes-open-solvated-versus-occluded-desolvated-active-sites/},
volume = {56},
year = {2017}
}
TY - JOUR
ID - 1403848
AU - Lišková, Veronika - Štěpánková, Veronika - Bednář, David - Brezovský, Jan - Prokop, Zbyněk - Chaloupková, Radka - Damborský, Jiří
PY - 2017
TI - Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites
JF - Angewandte Chemie International Edition
VL - 56
IS - 17
SP - 4719-4723
EP - 4719-4723
PB - WILEY-V C H VERLAG
SN - 14337851
KW - enantioselectivity
KW - enzyme catalysis
KW - enzymes
KW - molecular modeling
KW - protein engineering
UR - https://loschmidt.chemi.muni.cz/peg/publications/different-structural-origins-of-the-enantioselectivity-of-haloalkane-dehalogenases-toward-linear-%CE%B2-haloalkanes-open-solvated-versus-occluded-desolvated-active-sites/
N2 - The enzymatic enantiodiscrimination of linear bhaloalkanes is difficult because the simple structures of the substrates prevent directional interactions. Herein we describe two distinct molecular mechanisms for the enantiodiscrimination of the b-haloalkane 2-bromopentane by haloalkane dehalogenases. Highly enantioselective DbjA has an open, solvent-accessible active site, whereas the engineered enzyme DhaA31 has an occluded and less solvated cavity but shows similar enantioselectivity. The enantioselectivity of DhaA31 arises from steric hindrance imposed by two specific substitutions rather than hydration as in DbjA.
ER -
LIŠKOVÁ, Veronika, Veronika ŠTĚPÁNKOVÁ, David BEDNÁŘ, Jan BREZOVSKÝ, Zbyněk PROKOP, Radka CHALOUPKOVÁ a Jiří DAMBORSKÝ. Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites. Online. \textit{Angewandte Chemie International Edition}. WEINHEIM, GERMANY: WILEY-V C H VERLAG, 2017, roč.~56, č.~17, s.~4719-4723. ISSN~1433-7851. Dostupné z: https://dx.doi.org/10.1002/anie.201611193. [citováno 2024-04-24]
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