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The phosphatase activity of the isolated H-4-H-5 loop of Na+/K+ ATPase resides outside its ATP binding site

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12640%2F04%3A00005715" target="_blank" >RIV/60076658:12640/04:00005715 - isvavai.cz</a>

  • Alternative codes found

    RIV/67179843:_____/04:00031718 RIV/67985823:_____/04:00001314

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    The phosphatase activity of the isolated H-4-H-5 loop of Na+/K+ ATPase resides outside its ATP binding site

  • Original language description

    The structural stability of the large cytoplasmic domain (H-4-H-5 loop) of mouse alpha(1) subunit of Na+/K+ ATPase (L354-I777), the number and the location of its binding sites for 2'-3'-O-(trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and p-nitrophenylphosphate (pNPP) were investigated. C- and N-terminal shortening revealed that neither part of the phosphorylation (P)-domain are necessary for TNP-ATP binding. There is no indication of a second ATP site on the P-domain of the isolated loop, even though others reported previously of its existence by TNP-N(3)ADP affinity labeling of the full enzyme. Fluorescein isothiocyanate (FITC)-anisotropy measurements reveal a considerable stability of the nucleotide (N)-domain suggesting that it may not undergo a substantial conformational change upon ATP binding. The FITC modified loop showed only slightly diminished phosphatase activity, most likely due to a pNPP site on the N-domain around N398 whose mutation to D reduced the phosphatase a

  • Czech name

    Fosfatázová aktivita izolované H4-H5 smyčky NA/K ATPázy se vyskytuje mimo vazební místo pro ATP

  • Czech description

    Byla vyzkoumána strukturní stabilita velké cytoplasmatické smyčky myší a1 subjednotky Na/K-ATPázy, počet a umístění vazebních míst pro TNP-ATP a pNPP.

Classification

  • Type

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

  • CEP classification

    BO - Biophysics

  • 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

    2004

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    European Journal of Biochemistry

  • ISSN

    0014-2956

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    271

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

    3923-3936

  • UT code for WoS article

  • EID of the result in the Scopus database