Evidence map›Paper›PMID 29259125›Full record

ArticleThe Journal of biological chemistry2018

The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis.

Samuel S Bailey, Karl A P Payne, Karl Fisher, Stephen A Marshall, Matthew J Cliff, Reynard Spiess, David A Parker, Stephen E J Rigby, David Leys

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  5. Enzymatic Conversion of COChemical reviews · 2023
    Review
  6. EnzymaticACS sustainable chemistry & engineering · 2022
    Article
  7. Article
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  9. Article
  10. Article
  11. Review
  12. Article
  13. Structure and Mechanism ofACS catalysis · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
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

9 authors.

Samuel S BaileyFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
Karl A P PayneFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
Karl FisherFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
Stephen A MarshallFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
Matthew J CliffFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
Reynard SpiessFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
David A ParkerInnovation/Biodomain, Shell International Exploration and Production, Westhollow Technology Center, Houston, Texas 77082-3101.
Stephen E J RigbyFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and.
David LeysFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN, United Kingdom and david.leys@manchester.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/K017802/1Biotechnology and Biological Sciences Research Council BB/P000622/1
6 · The paper itself

Abstract

The UbiD family of reversible decarboxylases act on aromatic, heteroaromatic, and unsaturated aliphatic acids and utilize a prenylated flavin mononucleotide (prFMN) as cofactor, bound adjacent to a conserved Glu-Arg-Glu/Asp ionic network in the enzyme's active site. It is proposed that UbiD activation requires oxidative maturation of the cofactor, for which two distinct isomers, prFMN

Indexed as

Aspergillus nigerBinding SitesCarboxy-LyasesCatalysisCatalytic DomainConserved SequenceFlavin MononucleotideFungal ProteinsIsomerismKineticsOxidation-ReductionCarboxy-LyasesFlavin MononucleotideFungal Proteinscrystal structuredecarboxylaseenzyme catalysisenzyme mechanismenzyme structureEPRflavinoxidation-reduction (redox)prenylated flavin mononucleotide (prFMN)radicalUbiD

Identifiers

PMID29259125
PMCPMC5818171

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.