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Updated: May 15, 2026

Nucleoside Triphosphates - From Synthesis to Biochemical Characterization
Published on: April 3, 2014
Backbone nuclear magnetic resonance assignment of human deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase)
Johan Isaksson1, Esmeralda Woestenenk, Christer Sahlberg
1Drug Discovery and Design, Department of Chemistry, University of Tromsø, N-9037, Tromsø, Norway, johan.isaksson@uit.no.
Abstract:
Nuclear-associated deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) is an enzyme that hydrolyses deoxyuridine 5'-triphosphate (dUTP) to the monophosphate, thereby controlling the dUTP levels of the organism, which is essential for survival. Further, dUTPase is up-regulated in many cancers. Thus, dUTPase is a highly interesting potential drug target. We report, for the first time, the near complete nuclear magnetic resonance (NMR) spectroscopy (15)N/(13)C/(1)H backbone assignment of the 3 × 164 amino acids homo-trimer human dUTPase. Previously, only a handful backbone resonances belonging to the flexible C-terminus has been published for any protein in the dUTPase family.

