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. 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. |
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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. \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.
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