Evidence map›Paper›PMID 9572931›Full record

ArticleApplied and environmental microbiology1998

Identification and analysis of genes involved in anaerobic toluene metabolism by strain T1: putative role of a glycine free radical.

P W Coschigano, T S Wehrman, L Y Young

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural basis for anaerobic alkane activation by a multisubunit glycyl radical enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Identification of FeS clusters in the glycyl-radical enzyme benzylsuccinate synthase via EPR and Mössbauer spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  8. Article
  9. Kinetics for tautomerizations and dissociations of triglycine radical cations.Journal of the American Society for Mass Spectrometry · 2009
    Article
  10. Anaerobic catabolism of aromatic compounds: a genetic and genomic view.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  11. Anaerobic functionalization of unactivated C-H bonds.Current opinion in chemical biology · 2009
    Review
  12. Article
  13. Article
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  15. Article
  16. Article
  17. Article
  18. Recent advances in petroleum microbiology.Microbiology and molecular biology reviews : MMBR · 2003
    Review
  19. Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  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

3 authors at 2 institutions in 1 country.

P W CoschiganoDepartment of Biological Sciences, Ohio University, Athens 45701-2979, USA. Coschiga@ohiou.edu
T S Wehrman
L Y Young
Rutgers, The State University of New Jersey · USOhio University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The denitrifying strain T1 is able to grow with toluene serving as its sole carbon source. Two mutants which have defects in this toluene utilization pathway have been characterized. A clone has been isolated, and subclones which contain tutD and tutE, two genes in the T1 toluene metabolic pathway, have been generated. The tutD gene codes for an 864-amino-acid protein with a calculated molecular mass of 97,600 Da. The tutE gene codes for a 375-amino-acid protein with a calculated molecular mass of 41,300 Da. Two additional small open reading frames have been identified, but their role is not known. The TutE protein has homology to pyruvate formate-lyase activating enzymes. The TutD protein has homology to pyruvate formate-lyase enzymes, including a conserved cysteine residue at the active site and a conserved glycine residue that is activated to a free radical in this enzyme. Site-directed mutagenesis of these two conserved amino acids shows that they are also essential for the function of TutD.

Indexed as

Genes, BacterialAmino Acid SequenceAnaerobiosisCloning, MolecularFree RadicalsGlycineGram-Negative BacteriaMolecular Sequence DataMutagenesis, Site-DirectedStructure-Activity RelationshipTolueneFree RadicalsGlycineToluene

Identifiers

PMID9572931
PMCPMC106210
OpenAlexW2108062992

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.