Evidence map›Paper›PMID 10657253›Full record

ArticleThe Biochemical journal2000

Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids.

A Camacho, F Hidalgo-Zarco, V Bernier-Villamor, L M Ruiz-Pérez, D González-Pacanowska

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Is dUTPase Enzymatic Activity Truly Essential for Viability?International journal of molecular sciences · 2025
    Review
  2. Molecular Characterization of UL50 (dUTPase) Gene of Bovine Herpes Virus 1.Animals : an open access journal from MDPI · 2023
    Article
  3. Review
  4. Review
  5. Pyrimidine metabolism in schistosomes: A comparison with other parasites and the search for potential chemotherapeutic targets.Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · 2017
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Kinetic properties and inhibition of the dimeric dUTPase-dUDPase from Leishmania major.Protein science : a publication of the Protein Society · 2001
    Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

A CamachoInstituto de Parasitología y Biomedicina 'López-Neyra', Consejo Superior de Investigaciones Científicas, Calle Ventanilla 11, 18001-Granada, Spain.
F Hidalgo-Zarco
V Bernier-Villamor
L M Ruiz-Pérez
D González-Pacanowska
Instituto de Parasitología y Biomedicina "López - Neyra" · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously reported the presence, in the parasitic protozoan Leishmania major, of an enzyme involved in controlling intracellular dUTP levels. The gene encoding this enzyme has now been overexpressed in Escherichia coli, and the recombinant enzyme was purified to homogeneity. Biochemical and enzymic analyses of the Leishmania enzyme show that it is a novel nucleotidohydrolase highly specific for deoxyuridine 5'-triphosphate. The enzyme has proved to be a dimer by gel filtration and is able to hydrolyse both dUTP and dUDP quite efficiently, acting as a dUTP nucleotidohydrolase (dUTPase)-dUDP nucleotidohydrolase but has a limited capacity to act upon other nucleoside di- or triphosphates. The reaction products are dUMP and PP(i) when dUTP is the substrate and dUMP and P(i) in the case of dUDP. The enzyme is sensitive to inhibition by the reaction product dUMP but not by PP(i). dUTPase activity is highly dependent on Mg(2+) concentrations and markedly sensitive to the phosphatase inhibitor, NaF. In summary, Leishmania dUTPase appears to be markedly different to other proteins characterized previously that accomplish the same function.

Indexed as

AnimalsCationsDeoxyuracil NucleotidesDimerizationDiphosphatesEscherichia coliHydrolysisKineticsLeishmania majorMolecular WeightNucleotidesPhosphatesPhosphoric Monoester HydrolasesPlastidsPyrophosphatasesRecombinant Proteins2'-deoxyuridylic acidCationsDeoxyuracil Nucleotidesdeoxyuridine triphosphateDiphosphatesdUTP pyrophosphataseNucleotidesPhosphatesPhosphoric Monoester HydrolasesPyrophosphatasesRecombinant ProteinsSodium Fluoride

Identifiers

PMID10657253
PMCPMC1220836
OpenAlexW1993609178

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.