Evidence map›Paper›PMID 31342570›Full record

ReviewProtein science : a publication of the Protein Society2019

An overview of structure, function, and regulation of pyruvate kinases.

Norbert Schormann, Katherine L Hayden, Paul Lee, Surajit Banerjee, Debasish Chattopadhyay

Open access · greenAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
3.7field-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

92 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
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  7. Research Advances in Plant Pyruvate Kinase.International journal of molecular sciences · 2026
    Review
  8. Article
  9. Article
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  11. Sex differences in brain glucose metabolism and Alzheimer's disease risk and progression.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Developing the protein quality control system inSynthetic and systems biotechnology · 2026
    Article
  16. Article
  17. Article
  18. Bioactive Potentials of Endophytic FungusInternational journal of microbiology · 2026
    Article
  19. Article
  20. From Mutation to Manifestation: Evaluation of aAnimals : an open access journal from MDPI · 2025
    Article

32 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

5 authors at 3 institutions in 1 country.

Norbert SchormannDepartment of Biochemistry, University of Alabama at Birmingham, Birmingham, Alabama.
Katherine L HaydenDepartment of Chemistry and Physics, Birmingham-Southern College, Birmingham, Alabama.
Paul LeeDepartment of Medicine, University of Alabama at Birmingham, Birmingham, Alabama.
Surajit BanerjeeNortheastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne, Illinois.
Debasish ChattopadhyayDepartment of Medicine, University of Alabama at Birmingham, Birmingham, Alabama.ORCID 0000-0001-5262-9140
University of Alabama at Birmingham · USArgonne National Laboratory · USBirmingham–Southern College · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
NIGMS NIH HHS P30 GM124165NIH HHS S10 OD021527NIH HHS S10OD021527
6 · The paper itself

Abstract

In the last step of glycolysis Pyruvate kinase catalyzes the irreversible conversion of ADP and phosphoenolpyruvate to ATP and pyruvic acid, both crucial for cellular metabolism. Thus pyruvate kinase plays a key role in controlling the metabolic flux and ATP production. The hallmark of the activity of different pyruvate kinases is their tight modulation by a variety of mechanisms including the use of a large number of physiological allosteric effectors in addition to their homotropic regulation by phosphoenolpyruvate. Binding of effectors signals precise and orchestrated movements in selected areas of the protein structure that alter the catalytic action of these evolutionarily conserved enzymes with remarkably conserved architecture and sequences. While the diverse nature of the allosteric effectors has been discussed in the literature, the structural basis of their regulatory effects is still not well understood because of the lack of data representing conformations in various activation states. Results of recent studies on pyruvate kinases of different families suggest that members of evolutionarily related families follow somewhat conserved allosteric strategies but evolutionarily distant members adopt different strategies. Here we review the structure and allosteric properties of pyruvate kinases of different families for which structural data are available.

Indexed as

HumansProtein ConformationPyruvate KinasePyruvate Kinaseallosteric enzymecryptosporidiumcrystal structureglycolysisholo-enzymeprotein structurepyruvate kinase

Identifiers

PMID31342570
PMCPMC6739817
OpenAlexW2963976604

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.