Evidence map›Paper›PMID 32786413›Full record

ArticleBiochemistry2020

Solving the Conundrum: Widespread Proteins Annotated for Urea Metabolism in Bacteria Are Carboxyguanidine Deiminases Mediating Nitrogen Assimilation from Guanidine.

Nicholas O Schneider, Lambros J Tassoulas, Danyun Zeng, Amanda J Laseke, Nicholas J Reiter, Lawrence P Wackett, Martin St Maurice

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Deciphering guanidine assimilation and riboswitch-based gene regulation in cyanobacteria for synthetic biology applications.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Discovery of a NiNature communications · 2024
    Article
  10. Article
  11. Article
  12. Dinickel enzyme evolved to metabolize the pharmaceutical metformin and its implications for wastewater and human microbiomes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Canavanine utilizationRSC chemical biology · 2022
    Article
  19. Review
  20. Discovery of a NiNature · 2022
    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

7 authors at 2 institutions in 1 country.

Nicholas O SchneiderDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53201-1881, United States.
Lambros J TassoulasBioTechnology Institute, University of Minnesota, St. Paul, Minnesota 55108-6106, United States.
Danyun ZengDepartment of Chemistry, Marquette University, Milwaukee, Wisconsin 53201-1881, United States.
Amanda J LasekeDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53201-1881, United States.
Nicholas J ReiterDepartment of Chemistry, Marquette University, Milwaukee, Wisconsin 53201-1881, United States.
Lawrence P WackettBioTechnology Institute, University of Minnesota, St. Paul, Minnesota 55108-6106, United States.
Martin St MauriceDepartment of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53201-1881, United States.ORCID 0000-0002-6507-9528
Marquette University · USUniversity of Minnesota · US

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
Supplement to Existing Grant for the acquisition of a circular dichroism spectrometer at Marquette University's Chemistry DepartmentR01GM120572 · NIGMS · VANDERBILT UNIVERSITY · PI Nicholas J Reiter · 2017 to 2026
$3.2M
Investigation of the structure and function of urea amidolyaseR15GM097724 · NIGMS · MARQUETTE UNIVERSITY · PI ST. MAURICE, MARTIN RAOUL · 2012 to 2012
$346k
NIGMS NIH HHS R01 GM120572NIGMS NIH HHS R15 GM097724NIGMS NIH HHS T32 GM008347
6 · The paper itself

Abstract

Free guanidine is increasingly recognized as a relevant molecule in biological systems. Recently, it was reported that urea carboxylase acts preferentially on guanidine, and consequently, it was considered to participate directly in guanidine biodegradation. Urea carboxylase combines with allophanate hydrolase to comprise the activity of urea amidolyase, an enzyme predominantly found in bacteria and fungi that catalyzes the carboxylation and subsequent hydrolysis of urea to ammonia and carbon dioxide. Here, we demonstrate that urea carboxylase and allophanate hydrolase from

Indexed as

Allophanate HydrolaseAmmoniaCarbon-Nitrogen LigasesCatalysisCitrullinationGuanidineHydrolasesMetabolic Networks and PathwaysMolecular Sequence AnnotationNitrogenProtein SubunitsPseudomonas syringaeUreaAllophanate HydrolaseAmmoniaCarbon-Nitrogen LigasesGuanidineHydrolasesNitrogenProtein SubunitsUreaurea carboxylase (hydrolyzing)

Identifiers

PMID32786413
PMCPMC8184117
OpenAlexW3047453327

What OpenQuestion holds

Textmetadata
LicenceTDM
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.