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Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product and water mediated inhibition

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F02%3A00006262" target="_blank" >RIV/00216224:14310/02:00006262 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12640/02:00004511

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product and water mediated inhibition

  • Original language description

    The hydrolysis of haloalkanes to their corresponding alcohols and inorganic halides is catalysed by a/b-hydrolases called haloalkane dehalogenases. The study of haloalkane dehalogenases is vital for the development of these enzymes if they are to be utilized for bioremediation of organohalide-contaminated industrial waste. We report the kinetic and structural analysis of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) in complex with each of 1,2-dichloroethane and 1,2-dichloropropane and the reaction product of 1-chlorobutane turnover. Activity studies showed very weak, but detectable activity of LinB with 1,2-dichloroethane (0.012 nmol.s-1.mg-1 of enzyme) and 1,2-dichloropropane (0.027 nmol.s-1.mg-1 of enzyme). These activitiesare much weaker compared, for example, to activity of LinB with 1-chlorobutane (68.169 nmol.s-1.mg-1 of enzyme). Inhibition analysis reveals that both 1,2-dichloroethane and 1,2-dichloropropane act as simple competitive inhibitors of the

  • 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

    <a href="/en/project/ME%20276" target="_blank" >ME 276: Rational re-design of microbial enzymes involved in degradation of toxic organic pollutants.</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2002

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biochemistry

  • ISSN

    0006-2960

  • e-ISSN

  • Volume of the periodical

    41

  • Issue of the periodical within the volume

    15

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    4847

  • UT code for WoS article

  • EID of the result in the Scopus database