Evidence map›Paper›PMID 22730121›Full record

ArticleJournal of bacteriology2012

Defining sequence space and reaction products within the cyanuric acid hydrolase (AtzD)/barbiturase protein family.

Jennifer L Seffernick, Jasmine S Erickson, Stephan M Cameron, Seunghee Cho, Anthony G Dodge, Jack E Richman, Michael J Sadowsky, Lawrence P Wackett

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Bacterial Cyanuric Acid Hydrolase for Water Treatment.Applied and environmental microbiology · 2015
    Article
  12. The structure of the hexameric atrazine chlorohydrolase AtzA.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Crystallization and preliminary X-ray diffraction studies of cyanuric acid hydrolase from Azorhizobium caulinodans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  18. Article
  19. 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

8 authors at 2 institutions in 1 country.

Jennifer L SeffernickDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, Minnesota, USA.
Jasmine S Erickson
Stephan M Cameron
Seunghee Cho
Anthony G Dodge
Jack E Richman
Michael J Sadowsky
Lawrence P Wackett
University of Minnesota · USBiotechnology Institute · US

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
NIGMS NIH HHS GM08347)NIGMS NIH HHS T32 GM008347
6 · The paper itself

Abstract

Cyanuric acid hydrolases (AtzD) and barbiturases are homologous, found almost exclusively in bacteria, and comprise a rare protein family with no discernible linkage to other protein families or an X-ray structural class. There has been confusion in the literature and in genome projects regarding the reaction products, the assignment of individual sequences as either cyanuric acid hydrolases or barbiturases, and spurious connection of this family to another protein family. The present study has addressed those issues. First, the published enzyme reaction products of cyanuric acid hydrolase are incorrectly identified as biuret and carbon dioxide. The current study employed (13)C nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry to show that cyanuric acid hydrolase releases carboxybiuret, which spontaneously decarboxylates to biuret. This is significant because it revealed that homologous cyanuric acid hydrolases and barbiturases catalyze completely analogous reactions. Second, enzymes that had been annotated incorrectly in genome projects have been reassigned here by bioinformatics, gene cloning, and protein characterization studies. Third, the AtzD/barbiturase family has previously been suggested to consist of members of the amidohydrolase superfamily, a large class of metallohydrolases. Bioinformatics and the lack of bound metals both argue against a connection to the amidohydrolase superfamily. Lastly, steady-state kinetic measurements and observations of protein stability suggested that the AtzD/barbiturase family might be an undistinguished protein family that has undergone some resurgence with the recent introduction of industrial s-triazine compounds such as atrazine and melamine into the environment.

Indexed as

AmidohydrolasesAmino Acid SequenceAzorhizobium caulinodansBacteriaBacterial ProteinsBiuretBradyrhizobiumMolecular Sequence DataMoorellaPhylogenyRhizobium leguminosarumSequence AlignmentSequence Analysis, ProteinSubstrate SpecificityTriazinesAmidohydrolasesBacterial ProteinsbarbituraseBiuretcyanuric acidcyanuric acid amidohydrolaseTriazines

Identifiers

PMID22730121
PMCPMC3415516
OpenAlexW2125255744

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.