ArticleThe Biochemical journal2011
Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 29 citations in OpenAlex.
- dUTP pyrophosphatases from hyperthermophilic eubacterium and archaeon: Structural and functional examinations on the suitability for PCR application.Protein science : a publication of the Protein Society · 2024Article
- Enzyme kinetics of deoxyuridine triphosphatase from Western corn rootworm.BMC research notes · 2023Article
- Discovery of two new isoforms of the human DUT gene.Scientific reports · 2023Article
- Redox status of cysteines does not alter functional properties of human dUTPase but the Y54C mutation involved in monogenic diabetes decreases protein stability.Scientific reports · 2021Article
- Exploiting the Autozygome to Support Previously Published Mendelian Gene-Disease Associations: An Update.Frontiers in genetics · 2020Article
- Enzyme kinetics of dUTPase from the planarian Dugesia ryukyuensis.BMC research notes · 2019Article
- The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner.The Journal of biological chemistry · 2018Article
- Gene dosage effects in yeast support broader roles for the LOG1, HAM1 and DUT1 genes in detoxification of nucleotide analogues.PloS one · 2018Article
- Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids.Biotechnology journal · 2017Article
- A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe.Scientific reports · 2017Article
- Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.BMC research notes · 2015Article
- Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.Chemistry & biology · 2013Article
- GTP is the primary activator of the anti-HIV restriction factor SAMHD1.The Journal of biological chemistry · 2013Article
- Crystallization of Chlorella deoxyuridine triphosphatase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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8 authors at 1 institution in 1 country.
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Abstract
Genomes of all free-living organisms encode the enzyme dUTPase (dUTP pyrophosphatase), which plays a key role in preventing uracil incorporation into DNA. In the present paper, we describe the biochemical and structural characterization of DUT1 (Saccharomyces cerevisiae dUTPase). The hydrolysis of dUTP by DUT1 was strictly dependent on a bivalent metal cation with significant activity observed in the presence of Mg2+, Co2+, Mn2+, Ni2+ or Zn2+. In addition, DUT1 showed a significant activity against another potentially mutagenic nucleotide: dITP. With both substrates, DUT1 demonstrated a sigmoidal saturation curve, suggesting a positive co-operativity between the subunits. The crystal structure of DUT1 was solved at 2 Å resolution (1 Å=0.1 nm) in an apo state and in complex with the non-hydrolysable substrate α,β-imido dUTP or dUMP product. Alanine-replacement mutagenesis of the active-site residues revealed seven residues important for activity including the conserved triad Asp87/Arg137/Asp85. The Y88A mutant protein was equally active against both dUTP and UTP, indicating that this conserved tyrosine residue is responsible for discrimination against ribonucleotides. The structure of DUT1 and site-directed mutagenesis support a role of the conserved Phe142 in the interaction with the uracil base. Our work provides further insight into the molecular mechanisms of substrate selectivity and catalysis of dUTPases.
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