Structural and Functional Analysis of a Novel Haloalkane
Dehalogenase with Two Halide-Binding Sites.

J 2014

Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.

CHALOUPKOVÁ, Radka; T. PRUDNIKOVA; P. REZACOVA; Zbyněk PROKOP; Táňa KOUDELÁKOVÁ et al.

Základní údaje

Originální název

Structural and Functional Analysis of a Novel Haloalkane Dehalogenase with Two Halide-Binding Sites.

Autoři

Vydání

Acta Crystallographica D, 2014, 0907-4449

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 7.232 v roce 2013

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/14:00074206

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94

Štítky

AKR, rivok

Změněno: 11. 4. 2015 15:07, Ing. Andrea Mikešková

Anotace

V originále

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.

Návaznosti

GAP207/12/0775, projekt VaV

Název: Strukturně-funkční vztahy haloalkan dehalogenas

Investor: Grantová agentura ČR, Structure-functional Relationships of Haloalkane Dehalogenases

LO1214, projekt VaV

Název: Centrum pro výzkum toxických látek v prostředí (Akronym: RECETOX)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum pro výzkum toxických látek v prostředí

Citovat

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://doi.org/10.1107/S1399004714009018.

@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 = {https://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://doi.org/10.1107/S1399004714009018.

Přehled o publikaci