Evidence map›Paper›PMID 35377165›Full record

ArticleJournal of bacteriology2022

The Autonomous Glycyl Radical Protein GrcA Restores Activity to Inactive Full-Length Pyruvate Formate-Lyase

Michelle Kammel, R Gary Sawers

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 49% 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

9 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Journal of bacteriology · 2025
    Review
  5. Article
  6. Article
  7. Simultaneous glucose and xylose utilization by anApplied and environmental microbiology · 2024
    Article
  8. Article
  9. 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

2 authors at 1 institution in 1 country.

Michelle KammelInstitute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
R Gary SawersInstitute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.ORCID 0000-0003-0862-2683
Martin Luther University Halle-Wittenberg · DE

Funding

Martin Luther University Halle-Wittenberg
6 · The paper itself

Abstract

During glucose fermentation, Escherichia coli and many other microorganisms employ the glycyl radical enzyme (GRE) pyruvate formate-lyase (PflB) to catalyze the coenzyme A-dependent cleavage of pyruvate to formate and acetyl-coenzyme A (CoA). Due to its extreme reactivity, the radical in PflB must be controlled carefully and, once generated, is particularly susceptible to dioxygen. Exposure to oxygen of the radical on glycine residue 734 of PflB results in cleavage of the polypeptide chain and consequent inactivation of the enzyme. Two decades ago, a small 14-kDa protein called YfiD (now called autonomous

Indexed as

AcetyltransferasesEscherichia coli ProteinsAcetyl Coenzyme ACarbonEscherichia coliFormatesGlucoseGlycineOxygenPyruvatesAcetyl Coenzyme AAcetyltransferasesCarbonEscherichia coli Proteinsformate C-acetyltransferaseFormatesGlucoseGlycineOxygenPyruvatesYfiD protein, E colianaerobic metabolismautonomous glycyl radical cofactorglycyl radical enzymesoxygen sensitivitypyruvate formate-lyaseS-adenosylmethionine radical enzymes

Identifiers

PMID35377165
PMCPMC9112899
OpenAlexW4226250972

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.