Evidence map›Paper›PMID 16321143›Full record

ArticleThe Biochemical journal2006

Amplification and disruption of the phenylacetyl-CoA ligase gene of Penicillium chrysogenum encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N-acyltransferase.

Mónica Lamas-Maceiras, Inmaculada Vaca, Esther Rodríguez, Javier Casqueiro, Juan F Martín

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Subcellular localization of fungal specialized metabolites.Fungal biology and biotechnology · 2022
    Review
  7. Microorganisms · 2022
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  8. Review
  9. Article
  10. mSphere · 2020
    Article
  11. Review
  12. Genetic Modification ofMicroorganisms · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Peroxisomal acyl-CoA synthetases.Biochimica et biophysica acta · 2012
    Review
  18. Review
  19. Review
  20. 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

5 authors at 2 institutions in 1 country.

Mónica Lamas-MaceirasArea de Microbiología, Facultad de Ciencias Biológicas y Ambientales, Universidad de León, Campus de Vegazana, s/n, 24071 León, Spain.
Inmaculada Vaca
Esther Rodríguez
Javier Casqueiro
Juan F Martín
Universidad de León · ESInstituto de Biotecnología de León · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gene, phl, encoding a phenylacetyl-CoA ligase was cloned from a phage library of Penicillium chrysogenum AS-P-78. The presence of five introns in the phl gene was confirmed by reverse transcriptase-PCR. The phl gene encoded an aryl-CoA ligase closely related to Arabidopsis thaliana 4-coumaroyl-CoA ligase. The Phl protein contained most of the amino acids defining the aryl-CoA (4-coumaroyl-CoA) ligase substrate-specificity code and differed from acetyl-CoA ligase and other acyl-CoA ligases. The phl gene was not linked to the penicillin gene cluster. Amplification of phl in an autonomous replicating plasmid led to an 8-fold increase in phenylacetyl-CoA ligase activity and a 35% increase in penicillin production. Transformants containing the amplified phl gene were resistant to high concentrations of phenylacetic acid (more than 2.5 g/l). Disruption of the phl gene resulted in a 40% decrease in penicillin production and a similar reduction of phenylacetyl-CoA ligase activity. The disrupted mutants were highly susceptible to phenylacetic acid. Complementation of the disrupted mutants with the phl gene restored normal levels of penicillin production and resistance to phenylacetic acid. The phenylacetyl-CoA ligase encoded by the phl gene is therefore involved in penicillin production, although a second aryl-CoA ligase appears to contribute partially to phenylacetic acid activation. The Phl protein lacks a peptide-carrier-protein domain and behaves as an aryl-capping enzyme that activates phenylacetic acid and transfers it to the isopenicillin N acyltransferase. The Phl protein contains the peroxisome-targeting sequence that is also present in the isopenicillin N acyltransferase. The peroxisomal co-localization of these two proteins indicates that the last two enzymes of the penicillin pathway form a peroxisomal functional complex.

Indexed as

Gene DeletionAcyltransferasesAmino Acid MotifsAmino Acid SequenceBacteriophagesCarrier ProteinsCloning, MolecularCoenzyme A LigasesConserved SequenceDrug Resistance, FungalGene AmplificationGenetic Complementation TestGenomic LibraryMolecular Sequence DataMultigene FamilyPenicillin-Binding Proteinsacyl-CoA-6-aminopenicillanic acid acyltransferaseAcyltransferasesCarrier ProteinsCoenzyme A LigasesPenicillin-Binding ProteinsPenicillinsphenylacetate - CoA ligasePhenylacetatesphenylacetic acid

Identifiers

PMID16321143
PMCPMC1409706
OpenAlexW2091430601

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.