Different Structural Origins of the Enantioselectivity of
Haloalkane Dehalogenases toward Linear beta-Haloalkanes:
Open–Solvated versus Occluded–Desolvated Active Sites

J 2017

Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites

LIŠKOVÁ, Veronika, Veronika ŠTĚPÁNKOVÁ, David BEDNÁŘ, Jan BREZOVSKÝ, Zbyněk PROKOP et. al.

Basic information

Original name

Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear beta-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites

Authors

LIŠKOVÁ, Veronika (203 Czech Republic, belonging to the institution), Veronika ŠTĚPÁNKOVÁ (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Angewandte Chemie International Edition, WEINHEIM, GERMANY, WILEY-V C H VERLAG, 2017, 1433-7851

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 12.102

RIV identification code

RIV/00216224:14310/17:00095409

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.1002/anie.201611193

UT WoS

000398576000004

Keywords in English

enantioselectivity; enzyme catalysis; enzymes; molecular modeling; protein engineering

Abstract

V originále

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.

Links

GA16-06096S, research and development project

Name: Objasnění významu dynamických tunelů pro enzymatickou katalýzu: simulace a fluorescenční experimenty

Investor: Czech Science Foundation

GA17-24321S, research and development project

Name: Studium hydratace a flexibility enzymů pomocí pokročilých strukturních a biofyzikálních metod

Investor: Czech Science Foundation

LH14027, research and development project

Name: Nové koncepty a nástroje pro racionální design enzymů

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

LM2015051, research and development project

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

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

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

MUNI/M/1888/2014, interní kód MU

Name: Pokročilé hybridní metody studia transportních procesů v proteinech a jejich využití v designu biokatalyzátorů

Investor: Masaryk University, INTERDISCIPLINARY - Interdisciplinary research projects

Citovat

LIŠKOVÁ, Veronika, Veronika ŠTĚPÁNKOVÁ, David BEDNÁŘ, Jan BREZOVSKÝ, Zbyněk PROKOP, Radka CHALOUPKOVÁ and 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, vol. 56, No 17, p. 4719-4723. ISSN 1433-7851. Available from: https://dx.doi.org/10.1002/anie.201611193.

@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 and 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, vol.~56, No~17, p.~4719-4723. ISSN~1433-7851. Available from: https://dx.doi.org/10.1002/anie.201611193.

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