Crystallization and Preliminary X-ray Analysis of a Novel
Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94.

J 2009

Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94.

PRUDNIKOVA, T.; Tomáš MOZGA; P. REZACOVA; Radka CHALOUPKOVÁ; Yukari SATO et al.

Základní údaje

Originální název

Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94.

Název česky

Krystalizace a X-ray analýzy haloalkán dehalogenázy DbeA z bakterie Bradyrhizobium elkani USDA94.

Autoři

PRUDNIKOVA, T.; Tomáš MOZGA; P. REZACOVA; Radka CHALOUPKOVÁ; Yukari SATO; Yuji NAGATA; Y. BRYNDA; Michal KUTÝ; Jiří DAMBORSKÝ a Ivana KUTÁ-SMATANOVÁ

Vydání

Acta crystallographica. Section F Structural biology and crystallization communications, 2009, 1744-3091

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

Odkazy

URL

Impakt faktor

Impact factor: 0.551

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/09:00036387

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000264770000009

Klíčová slova anglicky

haloalkane dehalogenases; enzyme DbeA; Bradyrhizobium elkani USDA94.; crystaliyations;

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 3. 2012 11:02, prof. Mgr. Jiří Damborský, Dr.

Anotace

ORIG CZ

V originále

A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. This haloalkane dehalogenase is closely related to the DbjA enzyme from B. japonicum USDA110 (71% sequence identity), but has different biochemical properties. DbeA is generally less active and has a higher specificity towards brominated and iodinated compounds than DbjA. In order to understand the altered activity and specificity of DbeA, its mutant variant DbeA1, which carries the unique fragment of DbjA, was also constructed. Both wild-type DbeA and DbeA1 were crystallized using the sitting-drop vapour-diffusion method. The crystals of DbeA belonged to the primitive orthorhombic space group P212121, while the crystals of DbeA1 belonged to the monoclinic space group C2. Diffraction data were collected to 2.2 A resolution for both DbeA and DbeA1 crystals.

Česky

....

Návaznosti

LC06010, projekt VaV

Název: Centrum biokatalýzy a biotransformací

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum biokatalýzy a biotransformací

Citovat

PRUDNIKOVA, T.; Tomáš MOZGA; P. REZACOVA; Radka CHALOUPKOVÁ; Yukari SATO; Yuji NAGATA; Y. BRYNDA; Michal KUTÝ; Jiří DAMBORSKÝ a Ivana KUTÁ-SMATANOVÁ. Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94. Acta crystallographica. Section F Structural biology and crystallization communications. 2009, F65, č. 1, s. 353-356. ISSN 1744-3091.

@article{841905,
   author = {Prudnikova, T. and Mozga, Tomáš and Rezacova, P. and Chaloupková, Radka and Sato, Yukari and Nagata, Yuji and Brynda, Y. and Kutý, Michal and Damborský, Jiří and KutáandSmatanová, Ivana},
   article_number = {1},
   keywords = {haloalkane dehalogenases; enzyme DbeA; Bradyrhizobium elkani USDA94.; crystaliyations;},
   language = {eng},
   issn = {1744-3091},
   journal = {Acta crystallographica. Section F Structural biology and crystallization communications},
   title = {Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94.},
   url = {http://loschmidt.chemi.muni.cz/peg/pdf/acsf09.pdf},
   volume = {F65},
   year = {2009}
}

TY  - JOUR
ID  - 841905
AU  - Prudnikova, T. - Mozga, Tomáš - Rezacova, P. - Chaloupková, Radka - Sato, Yukari - Nagata, Yuji - Brynda, Y. - Kutý, Michal - Damborský, Jiří - Kutá-Smatanová, Ivana
PY  - 2009
TI  - Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94.
JF  - Acta crystallographica. Section F Structural biology and crystallization communications
VL  - F65
IS  - 1
SP  - 353-356
EP  - 353-356
SN  - 17443091
KW  - haloalkane dehalogenases
KW  - enzyme DbeA
KW  - Bradyrhizobium elkani USDA94.
KW  - crystaliyations;
UR  - http://loschmidt.chemi.muni.cz/peg/pdf/acsf09.pdf
N2  - A novel enzyme, DbeA, belonging to the haloalkane dehalogenase family (EC 3.8.1.5) was isolated from Bradyrhizobium elkani USDA94. This haloalkane dehalogenase is closely related to the DbjA enzyme from B. japonicum USDA110 (71% sequence identity), but has different biochemical properties. DbeA is generally less active and has a higher specificity towards brominated and iodinated compounds than DbjA. In order to understand the altered activity and specificity of DbeA, its mutant variant DbeA1, which carries the unique fragment of DbjA, was also constructed. Both wild-type DbeA and DbeA1 were crystallized using the sitting-drop vapour-diffusion method. The crystals of DbeA belonged to the primitive orthorhombic space group P212121, while the crystals of DbeA1 belonged to the monoclinic space group C2. Diffraction data were collected to 2.2 A resolution for both DbeA and DbeA1 crystals.
ER  -

PRUDNIKOVA, T.; Tomáš MOZGA; P. REZACOVA; Radka CHALOUPKOVÁ; Yukari SATO; Yuji NAGATA; Y. BRYNDA; Michal KUTÝ; Jiří DAMBORSKÝ a Ivana KUTÁ-SMATANOVÁ. Crystallization and Preliminary X-ray Analysis of a Novel Haloalkane Dehalogenase DbeA from Bradyrhizobium elkani USDA94. \textit{Acta crystallographica. Section F Structural biology and crystallization communications}. 2009, F65, č.~1, s.~353-356. ISSN~1744-3091.

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