Evidence map›Paper›PMID 23558683›Full record

ArticleThe Journal of biological chemistry2013

Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.

Yulia V Bertsova, Maria S Fadeeva, Vitaly A Kostyrko, Marina V Serebryakova, Alexander A Baykov, Alexander V Bogachev

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.7field-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

38 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Review
  3. Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  9. Article
  10. Article
  11. A Novel, NADH-Dependent Acrylate Reductase in Vibrio harveyi.Applied and environmental microbiology · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Microbiology (Reading, England) · 2020
    Article
  19. The effect of pH on Marinobacter hydrocarbonoclasticus denitrification pathway and nitrous oxide reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  20. Impact of NaJournal of bacteriology · 2020
    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

6 authors at 1 institution in 1 country.

Yulia V BertsovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Maria S FadeevaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Vitaly A KostyrkoBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Marina V SerebryakovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Alexander A BaykovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia.
Alexander V BogachevBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia. Electronic address: bogachev@genebee.msu.ru.
Lomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr-229 in Escherichia coli cells requires the presence of a co-expressed Vibrio apbE gene. The apbE genes cluster with genes for Na(+)-NQR and other FMN-binding flavoproteins in bacterial genomes and encode proteins with previously unknown function. Experiments with isolated NqrC and ApbE proteins confirmed that ApbE is the only protein factor required for NqrC flavinylation and also indicated that the reaction is Mg(2+)-dependent and proceeds with FAD but not FMN. Inactivation of the apbE gene in Klebsiella pneumoniae, wherein the nqr operon and apbE are well separated in the chromosome, resulted in a complete loss of the quinone reductase activity of Na(+)-NQR, consistent with its dependence on covalently bound flavin. Our data thus identify ApbE as a novel modifying enzyme, flavin transferase.

Indexed as

Amino Acid MotifsAmino Acid SequenceCatalysisElectron TransportEscherichia coliFlavin MononucleotideFlavinsGenetic VectorsKlebsiella pneumoniaeMagnesiumMass SpectrometryMolecular Sequence DataNucleotidyltransferasesOperonProtein BindingProtein Processing, Post-TranslationalFlavin MononucleotideFlavinsMagnesiumNucleotidyltransferasesPyrimidinesBacterial MetabolismFlavoproteinsFMNNa+-translocating NADH:Quinone OxidoreductasePost-translational ModificationRespiratory Chain

Identifiers

PMID23558683
PMCPMC3656284
OpenAlexW2106158884

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.