University of Oulu

Haikarainen T., Murthy S., Maksimainen M.M., Lehtiö L. (2018) Small-Molecule Screening Assay for Mono-ADP-Ribosyltransferases. In: Chang P. (eds) ADP-ribosylation and NAD+ Utilizing Enzymes. Methods in Molecular Biology, vol 1813. Humana Press, New York, NY

Small-molecule screening assay for mono-adp-ribosyltransferases

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Author: Haikarainen, Teemu1; Murthy, Sudarshan1; Maksimainen, Mirko M.1;
Organizations: 1Faculty of Biochemistry and Molecular Medicine, Biocenter Oulu, University of Oulu
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 0.2 MB)
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Language: English
Published: Humana Press, 2018
Publish Date: 2019-08-11


Mono-ADP-ribosyltransferases of the PARP/ARTD enzyme family are enzymes catalyzing the transfer of a single ADP-ribose unit to target proteins. The enzymes have various roles in vital cellular processes such as DNA repair and transcription, and many of the enzymes are linked to cancer-relevant functions. Thus inhibition of the enzymes is a potential way to discover and develop new drugs against cancer. Here we describe an activity-based screening assay for mono-ADP-ribosyltransferases. The assay utilizes the natural substrate of the enzymes, NAD+, and it is based on chemically converting the leftover substrate to a fluorophore and measuring its relative concentration after the enzymatic reaction. The assay is homogenous, robust, and cost-effective and, most importantly, applicable to mono-ADP-ribosyltransferases as well as poly-ADP-ribosyltransferases for screening of small-molecule inhibitors against the enzymes.

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Series: Methods in molecular biology
ISSN: 1064-3745
ISSN-E: 1940-6029
ISSN-L: 1064-3745
ISBN: 978-1-4939-8588-3
ISBN Print: 978-1-4939-8587-6
Issue: 1813
Pages: 237 - 244
DOI: 10.1007/978-1-4939-8588-3_16
Host publication: ADP-ribosylation and NAD+ utilizing enzymes
Host publication editor: Chang, Paul
Type of Publication: A3 Book chapter
Field of Science: 1182 Biochemistry, cell and molecular biology
Copyright information: © Springer Science+Business Media, LLC, part of Springer Nature 2018. This is a post-peer-review, pre-copyedit version of an article published in ADP-ribosylation and NAD+ Utilizing Enzymes. The final authenticated version is available online at: