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Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

The result's identifiers

  • Result code in 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>

  • Alternative codes found

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

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Acta Crystallographica

  • ISSN

    1744-3091

  • e-ISSN

  • Volume of the periodical

    69

  • Issue of the periodical within the volume

    Pt 3

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    4

  • Pages from-to

    284-287

  • UT code for WoS article

    000316745000014

  • EID of the result in the Scopus database