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
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DOI - Digital Object Identifier
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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
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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
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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
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EID of the result in the Scopus database
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