Evidence map›Paper›PMID 26961875›Full record

ArticleThe Journal of biological chemistry2016

Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD.

Ian Barr, John A Latham, Anthony T Iavarone, Teera Chantarojsiri, Jennifer D Hwang, Judith P Klinman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

65 citing papers in PubMed, 124 citations in OpenAlex.

  1. RadicalJournal of the American Chemical Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Diverse Protein Architectures and α-ACS chemical biology · 2022
    Article
  17. Article
  18. Review
  19. The BJournal of inorganic biochemistry · 2022
    Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Ian BarrFrom the Department of Chemistry, Department of Molecular and Cell Biology, and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720.ORCID http://orcid.org/0000-0003-1805-1415
John A LathamFrom the Department of Chemistry, California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720.
Anthony T IavaroneFrom the Department of Chemistry, California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720.
Teera ChantarojsiriFrom the Department of Chemistry.
Jennifer D HwangDepartment of Molecular and Cell Biology, and.
Judith P KlinmanFrom the Department of Chemistry, Department of Molecular and Cell Biology, and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720 klinman@berkeley.edu.
QB3 · USInstitute of Molecular and Cell Biology · RUUniversity of California, Berkeley · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
QUINOENZYMES: BIOGENESIS, STRUCTURE AND FUNCTIONR01GM039296 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 1988 to 2015
$6.3M
QTOF MASS SPECTROMETER: CELL MOLECULAR BIOLOGY, PROTEIN STRUCTURES10RR022393 · NCRR · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2006 to 2006
$499k
NCRR NIH HHS S10 RR022393NIGMS NIH HHS R01 GM039296NIGMS NIH HHS R35 GM118117
6 · The paper itself

Abstract

The radical S-adenosylmethionine (SAM) protein PqqE is predicted to function in the pyrroloquinoline quinone (PQQ) biosynthetic pathway via catalysis of carbon-carbon bond formation between a glutamate and tyrosine side chain within the small peptide substrate PqqA. We report here that PqqE activity is dependent on the accessory protein PqqD, which was recently shown to bind PqqA tightly. In addition, PqqE activity in vitro requires the presence of a flavodoxin- and flavodoxin reductase-based reduction system, with other reductants leading to an uncoupled cleavage of the co-substrate SAM. These results indicate that PqqE, in conjunction with PqqD, carries out the first step in PQQ biosynthesis: a radical-mediated formation of a new carbon-carbon bond between two amino acid side chains on PqqA.

Indexed as

Bacterial ProteinsCatalysisEndopeptidasesMycobacteriumBacterial ProteinsEndopeptidasesPqqA protein, Methylobacterium extorquensPqqD protein, Methylobacterium extorquensPqqE protein, Methylobacterium extorquensflavoproteiniron-sulfur proteinpeptidespost-translational modification (PTM)PQQradical SAMS-adenosylmethionine (SAM)SPASM domain

Identifiers

PMID26961875
PMCPMC4861456
OpenAlexW2296115795

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.