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Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues

Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues

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ERMERT, Susanne, Stephan M. HACKER, Alexander BUNTRU, Martin SCHEFFNER, Christof R. HAUCK, Andreas MARX, 2017. Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues. In: ChemBioChem. 18(4), pp. 378-381. ISSN 1439-4227. eISSN 1439-7633

@article{Ermert2017-02-16Diffe-38686, title={Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues}, year={2017}, doi={10.1002/cbic.201600590}, number={4}, volume={18}, issn={1439-4227}, journal={ChemBioChem}, pages={378--381}, author={Ermert, Susanne and Hacker, Stephan M. and Buntru, Alexander and Scheffner, Martin and Hauck, Christof R. and Marx, Andreas} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/38686"> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38686"/> <dc:creator>Scheffner, Martin</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-02T09:55:03Z</dcterms:available> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150914100631302-4485392-8"/> <dc:creator>Hauck, Christof R.</dc:creator> <dc:contributor>Hauck, Christof R.</dc:contributor> <dc:creator>Buntru, Alexander</dc:creator> <dc:contributor>Hacker, Stephan M.</dc:contributor> <dc:contributor>Scheffner, Martin</dc:contributor> <dc:creator>Ermert, Susanne</dc:creator> <dcterms:abstract xml:lang="eng">Monitoring the activity of ATP-consuming enzymes provides the basis for elucidating their modes of action and regulation. Although a number of ATP analogues have been developed for this, their scope is restricted because of the limited acceptance by respective enzymes. In order to clarify which kind of phosphate-modified ATP analogues are accepted by the α-β-phosphoanhydride-cleaving ubiquitin-activating enzyme 1 (UBA1) and the β-γ-phosphoanhydride-cleaving focal adhesion kinase (FAK), we tested phosphoramidate- and phosphoester-modified ATP analogues. UBA1 and FAK were able to convert phosphoramidate-modified ATP analogues, even with a bulky modification like biotin. In contrast, a phosphoester-modified analogue was poorly accepted. These results demonstrate that minor variations in the design of ATP analogues for monitoring ATP utilization have a significant impact on enzymatic acceptance.</dcterms:abstract> <dc:contributor>Ermert, Susanne</dc:contributor> <dcterms:title>Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues</dcterms:title> <dc:language>eng</dc:language> <dc:contributor>Buntru, Alexander</dc:contributor> <dc:creator>Marx, Andreas</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-02T09:55:03Z</dc:date> <dc:contributor>Marx, Andreas</dc:contributor> <dc:creator>Hacker, Stephan M.</dc:creator> <dcterms:issued>2017-02-16</dcterms:issued> </rdf:Description> </rdf:RDF>

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