| CHALOUPKOVÁ, Radka, T. PRUDNIKOVA, P. REZACOVA, Zbyněk PROKOP, Táňa KOUDELÁKOVÁ, Lukáš DANIEL, Jan BREZOVSKÝ, W. IKEDA-OHTSUBO, Y. SATO, M. KUTY, Y. NAGATA, I. KUTA SMATANOVA a Jiří DAMBORSKÝ. Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites. Acta Crystallographica D. 2014, roč. 70, July, s. 1884-1897. ISSN 0907-4449. Dostupné z: https://dx.doi.org/10.1107/S1399004714009018. |
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@article{1213460,
author = {Chaloupková, Radka and Prudnikova, T. and Rezacova, P. and Prokop, Zbyněk and Koudeláková, Táňa and Daniel, Lukáš and Brezovský, Jan and IkedaandOhtsubo, W. and Sato, Y. and Kuty, M. and Nagata, Y. and Kuta Smatanova, I. and Damborský, Jiří},
article_number = {July},
doi = {http://dx.doi.org/10.1107/S1399004714009018},
keywords = {haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94},
language = {eng},
issn = {0907-4449},
journal = {Acta Crystallographica D},
title = {Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.},
volume = {70},
year = {2014}
}
TY - JOUR
ID - 1213460
AU - Chaloupková, Radka - Prudnikova, T. - Rezacova, P. - Prokop, Zbyněk - Koudeláková, Táňa - Daniel, Lukáš - Brezovský, Jan - Ikeda-Ohtsubo, W. - Sato, Y. - Kuty, M. - Nagata, Y. - Kuta Smatanova, I. - Damborský, Jiří
PY - 2014
TI - Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.
JF - Acta Crystallographica D
VL - 70
IS - July
SP - 1884-1897
EP - 1884-1897
SN - 09074449
KW - haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94
N2 - Crystal structure of novel haloalkane dehalogenase DbeA revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift of substrate-specificity class and were accompanied by decrease of enzyme activity, stability and elimination of the substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step, mediated by lower basicity of the catalytic histidine.
ER -
CHALOUPKOVÁ, Radka, T. PRUDNIKOVA, P. REZACOVA, Zbyněk PROKOP, Táňa KOUDELÁKOVÁ, Lukáš DANIEL, Jan BREZOVSKÝ, W. IKEDA-OHTSUBO, Y. SATO, M. KUTY, Y. NAGATA, I. KUTA SMATANOVA a Jiří DAMBORSKÝ. Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites. \textit{Acta Crystallographica D}. 2014, roč.~70, July, s.~1884-1897. ISSN~0907-4449. Dostupné z: https://dx.doi.org/10.1107/S1399004714009018.
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