Evidence map›Paper›PMID 21203919›Full record

ArticleProtein & cell2010

Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases.

Ali Ryan, Chan-Ju Wang, Nicola Laurieri, Isaac Westwood, Edith Sim

Open access · bronzeAbstract read
In one paragraph

Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  14. Azoreductases in drug metabolism.British journal of pharmacology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Comparison of Metabolic Pathways in Escherichia coli by Using Genetic Algorithms.Computational and structural biotechnology journal · 2015
    Article
  19. Review
  20. 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 1 institution in 1 country.

Ali RyanDepartment of Pharmacology, University of Oxford, Mansfield Road, Oxford, OX1 3QT, UK.
Chan-Ju Wang
Nicola Laurieri
Isaac Westwood
Edith Sim
University of Oxford · GB

Funding

Cancer Research UK 6947
6 · The paper itself

Abstract

Azoreductases are involved in the bioremediation by bacteria of azo dyes found in waste water. In the gut flora, they activate azo pro-drugs, which are used for treatment of inflammatory bowel disease, releasing the active component 5-aminosalycilic acid. The bacterium P. aeruginosa has three azoreductase genes, paAzoR1, paAzoR2 and paAzoR3, which as recombinant enzymes have been shown to have different substrate specificities. The mechanism of azoreduction relies upon tautomerisation of the substrate to the hydrazone form. We report here the characterization of the P. aeruginosa azoreductase enzymes, including determining their thermostability, cofactor preference and kinetic constants against a range of their favoured substrates. The expression levels of these enzymes during growth of P. aeruginosa are altered by the presence of azo substrates. It is shown that enzymes that were originally described as azoreductases, are likely to act as NADH quinone oxidoreductases. The low sequence identities observed among NAD(P)H quinone oxidoreductase and azoreductase enzymes suggests convergent evolution.

Indexed as

BenzoquinonesCatalytic DomainEnzyme StabilityEvolution, MolecularFlavinsHot TemperatureKineticsMesalamineNADNADH, NADPH OxidoreductasesNADPNitroreductasesOsmolar ConcentrationOxidation-ReductionPhenylhydrazinesPhylogenyazoreductasebalsalazideBenzoquinonesFlavinsMesalamineNADNADH, NADPH OxidoreductasesNADPNitroreductasesPhenylhydrazinesquinone

Identifiers

PMID21203919
PMCPMC4875192
OpenAlexW2082939616

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.