Evidence map›Paper›PMID 41690591›Full record

ArticleThe Journal of biological chemistry2026

Identification of a distinct family of polyphosphate kinases relevant to energy homeostasis in Crenarchaeota.

Svenja Höfmann, Roman Kogay, Christian Schmerling, Christina Stracke, Felix Niemeyer, Torsten Schaller, Kira S Makarova, Eugene V Koonin, Jacky L Snoep, Christopher Bräsen and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. The roles and synthesis of inorganic polyphosphate inbioRxiv : the preprint server for biology · 2026
    Article
  2. 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

11 authors.

Svenja HöfmannMolecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany. Electronic address: svenja.hoefmann@uk-essen.de.
Roman KogayComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.
Christian SchmerlingMolecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Christina StrackeMolecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Felix NiemeyerFaculty of Chemistry (Organic Chemistry) and Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Essen, Germany.
Torsten SchallerFaculty of Chemistry (Organic Chemistry) and Center for Nanointegration Duisburg-Essen (CENIDE), University of Duisburg-Essen, Essen, Germany.
Kira S MakarovaComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.
Eugene V KooninComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, USA.
Jacky L SnoepDepartment of Biochemistry, Stellenbosch University, Stellenbosch, South Africa; Systems Biology Lab, AIMMS/A-LIFE, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.
Christopher BräsenMolecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Bettina SiebersMolecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany. Electronic address: bettina.siebers@uni-due.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inorganic polyphosphate (polyP), a linear polymer of orthophosphate residues, occurs in all three domains of life and plays key roles in metabolism and regulation. While polyP metabolism has been well studied in bacteria and eukaryotes, studies in archaea have been limited, where the polyphosphate kinases (PPKs) involved in polyP synthesis remained largely uncharacterized. Notably, members of the Crenarchaeota (Thermoproteota) lack homologs of bacterial PPKs. We identify two genes in the crenarchaeal model organism Sulfolobus acidocaldarius, (saci_2019 and saci_2020), previously annotated as thymidylate kinases, that together encode a heteromeric archaeal PPK (SaPPK3). Saci_2019 acts as the catalytic subunit (cPPK3), whereas Saci_2020 is a regulatory subunit (rPPK3) that enhances activity through oligomerization. SaPPK3 is reversible but strongly favors polyP-dependent nucleotide kinase activity, forming ATP from ADP and polyP. Kinetic modelling combined with quantitative

Indexed as

CrenarchaeotaEnergy MetabolismHomeostasisPhosphotransferases (Phosphate Group Acceptor)Sulfolobus acidocaldariusArchaeal ProteinsPhylogenyArchaeal ProteinsPhosphotransferases (Phosphate Group Acceptor)polyphosphate kinasearchaeaATP- polyphosphate metabolismenergy metabolisminorganic polyphosphatesPhylogeneticspolyphosphate kinasestructural analysisSulfolobus acidocaldarius

Identifiers

PMID41690591
PMCPMC12995831

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.