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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00074206" target="_blank" >RIV/00216224:14310/14:00074206 - isvavai.cz</a>

  • Alternative codes found

    RIV/67179843:_____/14:00430522 RIV/61388963:_____/14:00430522

  • Result on the web

    <a href="http://dx.doi.org/10.1107/S1399004714009018" target="_blank" >http://dx.doi.org/10.1107/S1399004714009018</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S1399004714009018" target="_blank" >10.1107/S1399004714009018</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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 haloalkanedehalogenases. 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.

  • 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

    2014

  • 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 D

  • ISSN

    0907-4449

  • e-ISSN

  • Volume of the periodical

    70

  • Issue of the periodical within the volume

    July

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    1884-1897

  • UT code for WoS article

    000338917000009

  • EID of the result in the Scopus database