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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
1997-9-3
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pubmed:abstractText |
CFTR-NBF-2 expressed and purified in fusion with the maltose-binding protein was shown to catalyse the reaction ATP-->ADP+Pi by three different assays, monitoring ATP turnover, formation of ADP and release of Pi (Km 86 microM, rate constant 0.37 min(-1)). The reaction product ADP inhibits this ATPase activity. In a similar manner the hydrolysis of GTP to GDP and Pi was demonstrated (Km 40 microM, rate constant 0.29 min(-1)). In the presence of AMP the ATPase reaction was superseded by the formation of two ADP from ATP and AMP. As typical for adenylate kinases a distinct AMP-binding site could be verified for CFTR-NBF-2 by the inability of TNP-ATP and AMP to compete for binding. All three enzymatic activities were inhibited by the symmetric double-substrate-mimicking inhibitor Ap5A. As NBF-2 plays a central role in CFTR channel opening and closing the results reported here are fundamental in understanding mechanisms of CFTR channel activity regulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Cystic Fibrosis Transmembrane...,
http://linkedlifedata.com/resource/pubmed/chemical/Dinucleoside Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/P(1),P(5)-di(adenosine-5'-)pentaphos...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
410
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
180-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9237625-Adenosine Diphosphate,
pubmed-meshheading:9237625-Adenosine Monophosphate,
pubmed-meshheading:9237625-Adenosine Triphosphatases,
pubmed-meshheading:9237625-Adenosine Triphosphate,
pubmed-meshheading:9237625-Adenylate Kinase,
pubmed-meshheading:9237625-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:9237625-Dinucleoside Phosphates,
pubmed-meshheading:9237625-Enzyme Inhibitors,
pubmed-meshheading:9237625-GTP Phosphohydrolases,
pubmed-meshheading:9237625-Guanosine Triphosphate,
pubmed-meshheading:9237625-Peptides,
pubmed-meshheading:9237625-Recombinant Fusion Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
A recombinant polypeptide model of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator functions as an active ATPase, GTPase and adenylate kinase.
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pubmed:affiliation |
Kinderklinik, Dr. von Haunerschen Kinderspital, Ludwig-Maximilians-Universität München, Germany. randak@clinbio.med.uni-muenchen.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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