Evidence map›Paper›PMID 17157819›Full record

ArticleBiochemical and biophysical research communications2007

The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1.

Jean Jakoncic, Yves Jouanneau, Christine Meyer, Vivian Stojanoff

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Review
  8. Engineering Rieske oxygenase activity one piece at a time.Current opinion in chemical biology · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Retuning Rieske-type oxygenases to expand substrate range.The Journal of biological chemistry · 2011
    Article
  15. Article
  16. Review
  17. 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 4 institutions in 2 countries.

Jean JakoncicBrookhaven National Laboratory, National Synchrotron Light Source, Upton, NY 11973, USA.
Yves Jouanneau
Christine Meyer
Vivian Stojanoff
Brookhaven National Laboratory · USCentre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRNational Synchrotron Light Source II

Funding

NIGMS NIH HHS Y01 GM000080
6 · The paper itself

Abstract

Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.

Indexed as

Binding SitesCatalytic DomainDioxygenasesModels, MolecularProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsSphingomonasSubstrate SpecificityDioxygenasesProtein Subunits

Identifiers

PMID17157819
PMCPMC1820764
OpenAlexW2016078245

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.