Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD⁺ analogues

• Sarah Wallrodt,
• Edward L. Simpson and
• Andreas Marx

Beilstein J. Org. Chem. 2017, 13, 495–501, doi:10.3762/bjoc.13.49

• -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. Keywords: ARTD; click chemistry; NAD+; poly(ADP

• -ribose and may branch every 20 to 50 monomers [8][9][10]. To date, only four ARTD members were found to accomplish the synthesis of PAR, namely the DNA-dependent ARTD1 and ARTD2 as well as the tankyrases ARTD5 and ARTD6 [2][3]. ARTD1 as the founding member is the best investigated enzyme of ARTDs and is

• undertaken to develop tools and assays for studying PARylation on a molecular level and to understand the complex processes and interactions of the involved ARTDs. Recently, the employment of NAD+ analogues resulted in the development of powerful applications for the determination and visualisation of ARTD