Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues
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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.
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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. 2017, 18(4), pp. 378-381. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201600590BibTex
@article{Ermert2017-02-16Diffe-38686, year={2017}, doi={10.1002/cbic.201600590}, title={Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues}, 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} }
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