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Haloalkane Dehalogenases From Marine Organisms

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F18%3A00101755" target="_blank" >RIV/00216224:14310/18:00101755 - isvavai.cz</a>

  • Alternative codes found

    RIV/00159816:_____/18:00070385

  • Result on the web

    <a href="http://dx.doi.org/10.1016/bs.mie.2018.03.005" target="_blank" >http://dx.doi.org/10.1016/bs.mie.2018.03.005</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/bs.mie.2018.03.005" target="_blank" >10.1016/bs.mie.2018.03.005</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Haloalkane Dehalogenases From Marine Organisms

  • Original language description

    Haloalkane dehalogenases degrade halogenated compounds to corresponding alcohols by a hydrolytic mechanism. These enzymes are being intensively investigated as model systems in experimental and in silico studies of enzyme mechanism and evolution, but also hold importance as useful biocatalysts for a number of biotechnological applications. Haloalkane dehalogenases originate from various organisms including bacteria (degraders, symbionts, or pathogens), eukaryotes, and archaea. Several members of this enzyme family have been found in marine organisms. The marine environment represents a good source of enzymes with novel properties, because of its diverse living conditions. A number of novel dehalogenases isolated from marine environments show interesting characteristics such as high activity, unusually broad substrate specificity, stability, or selectivity. In this chapter, the overview of haloalkane dehalogenases from marine organisms is presented and their characteristics are summarized together with an overview of the methods for their identification and biochemical characterization.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

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

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    MARINE ENZYMES AND SPECIALIZED METABOLISM, PT B

  • ISSN

    0076-6879

  • e-ISSN

  • Volume of the periodical

    605

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    49

  • Pages from-to

    203-251

  • UT code for WoS article

    000452360800008

  • EID of the result in the Scopus database