Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00066680" target="_blank" >RIV/00216224:14310/13:00066680 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68378050:_____/13:00398267 RIV/60076658:12520/13:43885237

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S1744309113002467" target="_blank" >http://dx.doi.org/10.1107/S1744309113002467</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S1744309113002467" target="_blank" >10.1107/S1744309113002467</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

Popis výsledku v původním jazyce

Haloalkane dehalogenases are microbial enzymes that convert a broad range of halogenated aliphatic compounds to their corresponding alcohols by the hydrolytic mechanism. These enzymes play an important role in the biodegradation of various environmentalpollutants. Haloalkane dehalogenase LinB isolated from a soil bacterium Sphingobium japonicum UT26 has a relatively broad substrate specificity and can be applied in bioremediation and biosensing of environmental pollutants. The LinB variants presented here, LinB32 and LinB70, were constructed with the goal of studying the effect of mutations on enzyme functionality. In the case of LinB32 (L117W), the introduced mutation leads to blocking of the main tunnel connecting the deeply buried active site withthe surrounding solvent. The other variant, LinB70 (L44I, H107Q), has the second halide-binding site in a position analogous to that in the related haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94.

Název v anglickém jazyce

Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

Popis výsledku anglicky

Haloalkane dehalogenases are microbial enzymes that convert a broad range of halogenated aliphatic compounds to their corresponding alcohols by the hydrolytic mechanism. These enzymes play an important role in the biodegradation of various environmentalpollutants. Haloalkane dehalogenase LinB isolated from a soil bacterium Sphingobium japonicum UT26 has a relatively broad substrate specificity and can be applied in bioremediation and biosensing of environmental pollutants. The LinB variants presented here, LinB32 and LinB70, were constructed with the goal of studying the effect of mutations on enzyme functionality. In the case of LinB32 (L117W), the introduced mutation leads to blocking of the main tunnel connecting the deeply buried active site withthe surrounding solvent. The other variant, LinB70 (L44I, H107Q), has the second halide-binding site in a position analogous to that in the related haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica

ISSN

1744-3091

e-ISSN

—

Svazek periodika

69

Číslo periodika v rámci svazku

Pt 3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

284-287

Kód UT WoS článku

000316745000014

EID výsledku v databázi Scopus

—