Evidence map›Paper›PMID 18502868›Full record

ArticleJournal of bacteriology2008

Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB.

Mariëlle J H Moonen, Nanne M Kamerbeek, Adrie H Westphal, Sjef A Boeren, Dick B Janssen, Marco W Fraaije, Willem J H van Berkel

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Bacterial catabolism of acetovanillone, a lignin-derived compound.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. HarnessingMicroorganisms · 2022
    Article
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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.

Mariëlle J H MoonenLaboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands.
Nanne M Kamerbeek
Adrie H Westphal
Sjef A Boeren
Dick B Janssen
Marco W Fraaije
Willem J H van Berkel
Wageningen University & Research · NLUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB is known to proceed through the intermediate formation of hydroquinone. Here, we provide evidence that hydroquinone is further degraded through 4-hydroxymuconic semialdehyde and maleylacetate to beta-ketoadipate. The P. fluorescens ACB genes involved in 4-hydroxyacetophenone utilization were cloned and characterized. Sequence analysis of a 15-kb DNA fragment showed the presence of 14 open reading frames containing a gene cluster (hapCDEFGHIBA) of which at least four encoded enzymes are involved in 4-hydroxyacetophenone degradation: 4-hydroxyacetophenone monooxygenase (hapA), 4-hydroxyphenyl acetate hydrolase (hapB), 4-hydroxymuconic semialdehyde dehydrogenase (hapE), and maleylacetate reductase (hapF). In between hapF and hapB, three genes encoding a putative intradiol dioxygenase (hapG), a protein of the Yci1 family (hapH), and a [2Fe-2S] ferredoxin (hapI) were found. Downstream of the hap genes, five open reading frames are situated encoding three putative regulatory proteins (orf10, orf12, and orf13) and two proteins possibly involved in a membrane efflux pump (orf11 and orf14). Upstream of hapE, two genes (hapC and hapD) were present that showed weak similarity with several iron(II)-dependent extradiol dioxygenases. Based on these findings and additional biochemical evidence, it is proposed that the hapC and hapD gene products are involved in the ring cleavage of hydroquinone.

Indexed as

AcetophenonesAdipatesBacterial ProteinsCloning, MolecularDNA, BacterialEnzymesFatty Acids, UnsaturatedFerredoxinsHydroquinonesMagnetic Resonance SpectroscopyMaleatesMembrane Transport ProteinsMetabolic Networks and PathwaysMolecular Sequence DataMultigene FamilyOpen Reading Frames3-oxoadipic acid4-hydroxyacetophenone4-hydroxyacetophenone monooxygenaseAcetophenonesAdipatesBacterial Proteins(chloro)hydroquinone 1, 2-dioxygenaseDNA, BacterialEnzymesextradiol dioxygenaseFatty Acids, UnsaturatedFerredoxinshydroquinoneHydroquinoneshydroxymuconic semialdehydeMaleatesmaleoylacetic acidmaleylacetate reductaseMembrane Transport ProteinsOxidoreductases Acting on CH-CH Group DonorsOxygenases

Identifiers

PMID18502868
PMCPMC2493259
OpenAlexW2155369995

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.