Evidence map›Paper›PMID 27294321›Full record

ArticleNature chemical biology2016

A conserved phosphatase destroys toxic glycolytic side products in mammals and yeast.

François Collard, Francesca Baldin, Isabelle Gerin, Jennifer Bolsée, Gaëtane Noël, Julie Graff, Maria Veiga-da-Cunha, Vincent Stroobant, Didier Vertommen, Amina Houddane and 4 more

Open access · greenAbstract read
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In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
12.3field-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

57 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
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  4. The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026
    Review
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  8. AJournal of bacteriology · 2025
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  10. CLYBL averts vitamin BNature chemical biology · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 2 countries.

François CollardWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Francesca BaldinWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Isabelle GerinWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Jennifer BolséeWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Gaëtane NoëlWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Julie GraffWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Maria Veiga-da-CunhaWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Vincent StroobantLudwig Institute for Cancer Research, Brussels, Belgium.
Didier VertommenProtein Phosphorylation Unit, de Duve Institute, Université Catholique de Louvain, Brussels, Belgium.
Amina HouddaneProtein Phosphorylation Unit, de Duve Institute, Université Catholique de Louvain, Brussels, Belgium.
Mark H RiderProtein Phosphorylation Unit, de Duve Institute, Université Catholique de Louvain, Brussels, Belgium.
Carole L LinsterLuxembourg Centre for Systems Biomedicine, University of Luxembourg, Esch-sur-Alzette, Luxembourg.
Emile Van SchaftingenWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
Guido T BommerWalloon Excellence in Lifesciences and Biotechnology (WELBIO), Brussels, Belgium.
UCLouvain · BEde Duve Institute · BELudwig Cancer Research · BEUniversity of Luxembourg · LUWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metabolic enzymes are very specific. However, most of them show weak side activities toward compounds that are structurally related to their physiological substrates, thereby producing side products that may be toxic. In some cases, 'metabolite repair enzymes' eliminating side products have been identified. We show that mammalian glyceraldehyde 3-phosphate dehydrogenase and pyruvate kinase, two core glycolytic enzymes, produce 4-phosphoerythronate and 2-phospho-L-lactate, respectively. 4-Phosphoerythronate strongly inhibits an enzyme of the pentose phosphate pathway, whereas 2-phospho-L-lactate inhibits the enzyme producing the glycolytic activator fructose 2,6-bisphosphate. We discovered that a single, widely conserved enzyme, known as phosphoglycolate phosphatase (PGP) in mammals, dephosphorylates both 4-phosphoerythronate and 2-phospho-L-lactate, thereby preventing a block in the pentose phosphate pathway and glycolysis. Its yeast ortholog, Pho13, similarly dephosphorylates 4-phosphoerythronate and 2-phosphoglycolate, a side product of pyruvate kinase. Our work illustrates how metabolite repair enzymes can make up for the limited specificity of metabolic enzymes and permit high flux in central metabolic pathways.

Indexed as

GlycolysisGlycolatesHCT116 CellsHumansLactatesPentose Phosphate PathwayPhosphoric Monoester HydrolasesPhosphorylationPyruvate KinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificitySugar Acids2-phospholactic acid4-phosphoerythronateGlycolatesLactatesPho13 protein, S cerevisiaephosphoglycolatephosphoglycolate phosphatasePhosphoric Monoester HydrolasesPyruvate KinaseSaccharomyces cerevisiae ProteinsSugar Acids

Identifiers

PMID27294321
OpenAlexW2438481482

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.