TY - JOUR A1 - Wallrodt, Sarah A1 - Simpson, Edward L. A1 - Marx, Andreas T1 - Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues JF - Beilstein Journal of Organic Chemistry PY - 2017/// VL - 13 SP - 495 EP - 501 SN - 1860-5397 DO - 10.3762/bjoc.13.49 PB - Beilstein-Institut JA - Beilstein J. Org. Chem. UR - https://doi.org/10.3762/bjoc.13.49 KW - ARTD KW - click chemistry KW - NAD+ KW - poly(ADP-ribose) KW - posttranslational modification N2 - 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. ER -