Evidence map›Paper›PMID 28128209›Full record

ArticleNature communications2017

Enzyme I facilitates reverse flux from pyruvate to phosphoenolpyruvate in Escherichia coli.

Christopher P Long, Jennifer Au, Nicholas R Sandoval, Nikodimos A Gebreselassie, Maciek R Antoniewicz

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 55 citations in OpenAlex.

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  15. High-resolutionNature protocols · 2019
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  19. Dissecting the genetic and metabolic mechanisms of adaptation to the knockout of a major metabolic enzyme inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

5 authors at 1 institution in 1 country.

Christopher P LongDepartment of Chemical and Biomolecular Engineering, Metabolic Engineering and Systems Biology Laboratory, University of Delaware, Newark Delaware 19716, USA.ORCID 0000-0003-1007-417X
Jennifer AuDepartment of Chemical and Biomolecular Engineering, Metabolic Engineering and Systems Biology Laboratory, University of Delaware, Newark Delaware 19716, USA.
Nicholas R SandovalDepartment of Chemical and Biomolecular Engineering, Metabolic Engineering and Systems Biology Laboratory, University of Delaware, Newark Delaware 19716, USA.
Nikodimos A GebreselassieDepartment of Chemical and Biomolecular Engineering, Metabolic Engineering and Systems Biology Laboratory, University of Delaware, Newark Delaware 19716, USA.
Maciek R AntoniewiczDepartment of Chemical and Biomolecular Engineering, Metabolic Engineering and Systems Biology Laboratory, University of Delaware, Newark Delaware 19716, USA.
University of Delaware · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) consists of cascading phosphotransferases that couple the simultaneous import and phosphorylation of a variety of sugars to the glycolytic conversion of phosphoenolpyruvate (PEP) to pyruvate. As the primary route of glucose uptake in E. coli, the PTS plays a key role in regulating central carbon metabolism and carbon catabolite repression, and is a frequent target of metabolic engineering interventions. Here we show that Enzyme I, the terminal phosphotransferase responsible for the conversion of PEP to pyruvate, is responsible for a significant in vivo flux in the reverse direction (pyruvate to PEP) during both gluconeogenic and glycolytic growth. We use

Indexed as

Carbohydrate MetabolismEscherichia coliEscherichia coli ProteinsGene Knockout TechniquesGenes, BacterialGlucoseMetabolic EngineeringMonosaccharide Transport ProteinsPhosphoenolpyruvatePhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationPyruvic AcidEscherichia coli ProteinsGlucosemannitol PTS permease, E coliMonosaccharide Transport ProteinsPhosphoenolpyruvatePhosphoenolpyruvate Sugar Phosphotransferase SystemPyruvic Acid

Identifiers

PMID28128209
PMCPMC5290146
OpenAlexW2582463890

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.