Dynamics and Hydration Explain Failed Functional Transformation
in Dehalogenase Design.

J 2014

Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.

SYKORA, J., Jan BREZOVSKÝ, Táňa KOUDELÁKOVÁ, M. LAHODA, Andrea FOŘTOVÁ et. al.

Basic information

Original name

Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.

Authors

SYKORA, J. (203 Czech Republic), Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution), Táňa KOUDELÁKOVÁ (203 Czech Republic, belonging to the institution), M. LAHODA (112 Belarus), Andrea FOŘTOVÁ (203 Czech Republic, belonging to the institution), T. CHERNOVETS (112 Belarus), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Veronika ŠTĚPÁNKOVÁ (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), I. KUTA SMATANOVA (203 Czech Republic), M. HOF (276 Germany) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nature Chemical Biology, 2014, 1552-4450

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 12.996

RIV identification code

RIV/00216224:14310/14:00074209

Organization unit

Faculty of Science

UT WoS

000336238200008

Keywords in English

haloalkane dehalogenase

Abstract

V originále

We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.

Links

EE2.3.30.0037, research and development project

Name: Zaměstnáním nejlepších mladých vědců k rozvoji mezinárodní spolupráce

GAP503/12/0572, research and development project

Name: Konstrukce syntetické metabolické dráhy pro degradaci důležitého environmentálního polutantu proteinovým a metabolickým inženýrstvím

Investor: Czech Science Foundation

LO1214, research and development project

Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

SYKORA, J., Jan BREZOVSKÝ, Táňa KOUDELÁKOVÁ, M. LAHODA, Andrea FOŘTOVÁ, T. CHERNOVETS, Radka CHALOUPKOVÁ, Veronika ŠTĚPÁNKOVÁ, Zbyněk PROKOP, I. KUTA SMATANOVA, M. HOF and Jiří DAMBORSKÝ. Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design. Nature Chemical Biology. 2014, vol. 10, No 6, p. 428-430. ISSN 1552-4450.

@article{1213468,
   author = {Sykora, J. and Brezovský, Jan and Koudeláková, Táňa and Lahoda, M. and Fořtová, Andrea and Chernovets, T. and Chaloupková, Radka and Štěpánková, Veronika and Prokop, Zbyněk and Kuta Smatanova, I. and Hof, M. and Damborský, Jiří},
   article_number = {6},
   keywords = {haloalkane dehalogenase},
   language = {eng},
   issn = {1552-4450},
   journal = {Nature Chemical Biology},
   title = {Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.},
   volume = {10},
   year = {2014}
}

TY  - JOUR
ID  - 1213468
AU  - Sykora, J. - Brezovský, Jan - Koudeláková, Táňa - Lahoda, M. - Fořtová, Andrea - Chernovets, T. - Chaloupková, Radka - Štěpánková, Veronika - Prokop, Zbyněk - Kuta Smatanova, I. - Hof, M. - Damborský, Jiří
PY  - 2014
TI  - Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design.
JF  - Nature Chemical Biology
VL  - 10
IS  - 6
SP  - 428-430
EP  - 428-430
SN  - 15524450
KW  - haloalkane dehalogenase
N2  - We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.
ER  -

SYKORA, J., Jan BREZOVSKÝ, Táňa KOUDELÁKOVÁ, M. LAHODA, Andrea FOŘTOVÁ, T. CHERNOVETS, Radka CHALOUPKOVÁ, Veronika ŠTĚPÁNKOVÁ, Zbyněk PROKOP, I. KUTA SMATANOVA, M. HOF and Jiří DAMBORSKÝ. Dynamics and Hydration Explain Failed Functional Transformation in Dehalogenase Design. \textit{Nature Chemical Biology}. 2014, vol.~10, No~6, p.~428-430. ISSN~1552-4450.

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