Publikation: Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues
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ADP-ribosyl transferases with diphtheria toxin homology (ARTDs) catalyse the covalent addition of ADP-ribose onto different acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the complex poly(ADP-ribose) biopolymer. The investigation of this posttranslational modification is important due to its involvement in cancer and other diseases. Lately, metabolic labelling approaches comprising different reporter-modified NAD+ building blocks have stimulated and enriched proteomic studies and imaging applications of ADP-ribosylation processes. Herein, we compare the substrate scope and applicability of different NAD+ analogues for the investigation of the polymer-synthesising enzymes ARTD1, ARTD2, ARTD5 and ARTD6. By varying the site and size of the NAD+ modification, suitable probes were identified for each enzyme. This report provides guidelines for choosing analogues for studying poly(ADP-ribose)-synthesising enzymes.
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WALLRODT, Sarah, Edward L. SIMPSON, Andreas MARX, 2017. Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues. In: Beilstein Journal of Organic Chemistry. 2017, 13, pp. 495-501. eISSN 1860-5397. Available under: doi: 10.3762/bjoc.13.49BibTex
@article{Wallrodt2017-03-10Inves-38625, year={2017}, doi={10.3762/bjoc.13.49}, title={Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD<sup>+</sup> analogues}, volume={13}, journal={Beilstein Journal of Organic Chemistry}, pages={495--501}, author={Wallrodt, Sarah and Simpson, Edward L. and Marx, Andreas} }
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