Evidence map›Paper›PMID 34260306›Full record

ReviewApplied and environmental microbiology2021

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily.

M E Arnold, I Kaplieva-Dudek, I Heker, R U Meckenstock

Open access · hybridAbstract readReview
In one paragraph

Review in Applied and environmental microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Anaerobic degradation of polycyclic aromatic hydrocarbons.Applied and environmental microbiology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

4 authors at 1 institution in 1 country.

M E Arnold *Environmental Microbiology and Biotechnology (EMB), University of Duisburg-Essengrid.5718.b, Essen, Germany.
I Kaplieva-Dudek *Environmental Microbiology and Biotechnology (EMB), University of Duisburg-Essengrid.5718.b, Essen, Germany.
I HekerEnvironmental Microbiology and Biotechnology (EMB), University of Duisburg-Essengrid.5718.b, Essen, Germany.
R U MeckenstockEnvironmental Microbiology and Biotechnology (EMB), University of Duisburg-Essengrid.5718.b, Essen, Germany.
University of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aryl coenzyme A (CoA) ligases belong to class I of the adenylate-forming enzyme superfamily (ANL superfamily). They catalyze the formation of thioester bonds between aromatic compounds and CoA and occur in nearly all forms of life. These ligases are involved in various metabolic pathways degrading benzene, toluene, ethylbenzene, and xylene (BTEX) or polycyclic aromatic hydrocarbons (PAHs). They are often necessary to produce the central intermediate benzoyl-CoA that occurs in various anaerobic pathways. The substrate specificity is very diverse between enzymes within the same class, while the dependency on Mg

Indexed as

Bacterial ProteinsCoenzyme A LigasesAdenosine MonophosphateAerobiosisAnaerobiosisBacteriaSubstrate SpecificityAdenosine MonophosphateBacterial ProteinsCoenzyme A Ligases2-naphthoate-CoA ligase2-phenanthrene-CoA ligaseadenylate-forming enzymesANL superfamilyaryl-CoA ligasesbenzoate-CoA ligaseBTEX degradationhydrocarbon degradationPAH degradationphenylacetate-CoA ligase

Identifiers

PMID34260306
PMCPMC8388817
OpenAlexW3181100924

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.