Evidence map›Paper›PMID 33830741›Full record

ArticleBiochemistry2021

Discovery of a New, Recurrent Enzyme in Bacterial Phosphonate Degradation: (

Erika Zangelmi, Toda Stanković, Marco Malatesta, Domenico Acquotti, Katharina Pallitsch, Alessio Peracchi

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.1field-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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Transcriptome analysis ofMicrobiology spectrum · 2026
    Article
  2. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
    Article
  3. Article
  4. OftenFrontiers in microbiology · 2025
    Article
  5. Laundry IsolateMicroorganisms · 2024
    Article
  6. Glyphosate-Induced Phosphonatase Operons in Soil Bacteria of the GenusInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Growth Increase in the Herbaceous PlantPlants (Basel, Switzerland) · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

6 authors at 2 institutions in 2 countries.

Erika ZangelmiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, I-43124 Parma, Italy.
Toda StankovićInstitute of Organic Chemistry, University of Vienna, Währingerstrasse 38, A-1090 Vienna, Austria.
Marco MalatestaDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, I-43124 Parma, Italy.
Domenico AcquottiCentro di Servizi e Misure "Giuseppe Casnati", University of Parma, I-43124 Parma, Italy.
Katharina PallitschInstitute of Organic Chemistry, University of Vienna, Währingerstrasse 38, A-1090 Vienna, Austria.ORCID 0000-0003-2648-1044
Alessio PeracchiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, I-43124 Parma, Italy.ORCID 0000-0003-3254-4099
University of Parma · ITUniversity of Vienna · AT

Funding

Austrian Science Fund FWF P 27987
6 · The paper itself

Abstract

Phosphonates represent an important source of bioavailable phosphorus in certain environments. Accordingly, many microorganisms (particularly marine bacteria) possess catabolic pathways to degrade these molecules. One example is the widespread hydrolytic route for the breakdown of 2-aminoethylphosphonate (AEP, the most common biogenic phosphonate). In this pathway, the aminotransferase PhnW initially converts AEP into phosphonoacetaldehyde (PAA), which is then cleaved by the hydrolase PhnX to yield acetaldehyde and phosphate. This work focuses on a pyridoxal 5'-phosphate-dependent enzyme that is encoded in >13% of the bacterial gene clusters containing the

Indexed as

VibrioAminoethylphosphonic AcidAmmonia-LyasesBacterial ProteinsOrganophosphonatesSubstrate SpecificityAminoethylphosphonic AcidAmmonia-LyasesBacterial ProteinsOrganophosphonates

Identifiers

PMID33830741
PMCPMC8154272
OpenAlexW3149016991

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.