Evidence map›Paper›PMID 39393572›Full record

ArticleThe Journal of biological chemistry2024

Structure function analysis of ADP-dependent cyanobacterial phosphofructokinase reveals new phylogenetic grouping in the PFK-A family.

Lu Shen, Carmen Peraglie, David Podlesainski, Christina Stracke, Ravi Shankar Ojha, Frauke Caliebe, Markus Kaiser, Karl Forchhammer, Martin Hagemann, Kirstin Gutekunst and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2024. 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 return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026
    Review
  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

13 authors.

Lu ShenMolecular 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.
Carmen PeraglieMolecular 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.
David PodlesainskiChemical Biology, Centre of Medical Biotechnology (ZMB), Faculty of Biology, 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.
Ravi Shankar OjhaMolecular 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.
Frauke CaliebeMolekulare Pflanzenphysiologie, University of Kassel, Kassel, Germany.
Markus KaiserChemical Biology, Centre of Medical Biotechnology (ZMB), Faculty of Biology, University of Duisburg-Essen, Essen, Germany.
Karl ForchhammerMicrobiology, University of Tübingen, Tübingen, Germany.
Martin HagemannPlant Physiology, University of Rostock, Rostock, Germany.
Kirstin GutekunstMolekulare Pflanzenphysiologie, University of Kassel, Kassel, Germany.
Jacky L SnoepBiochemistry, University of Stellenbosch, Stellenbosch, South Africa; Molecular Cell Biology, 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. Electronic address: christopher.braesen@uni-due.de.
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

Depending on the light conditions, photosynthetic organisms switch between carbohydrate synthesis or breakdown, for which the reversibility of carbohydrate metabolism, including glycolysis, is essential. Kinetic regulation of phosphofructokinase (PFK), a key-control point in glycolysis, was studied in the cyanobacterium Synechocystis sp. PCC 6803. The two PFK iso-enzymes (PFK- A1, PFK-A2), were found to use ADP instead of ATP, and have similar kinetic characteristics, but differ in their allosteric regulation. PFK-A1 is inhibited by 3-phosphoglycerate, a product of the Calvin-Benson-Bassham cycle, while PFK-A2 is inhibited by ATP, which is provided by photosynthesis. This regulation enables cyanobacteria to switch PFK off in light, and on in darkness. ADP dependence has not been reported before for the PFK-A enzyme family and was thought to be restricted to the PFK-B ribokinase superfamily. Phosphate donor specificity within the PFK-A family could be related to specific binding motifs in ATP-, ADP-, and PPi-dependent PFK-As. Phylogenetic analysis revealed a distribution of ADP-PFK-As in cyanobacteria and in a few alphaproteobacteria, which was confirmed in enzymatic studies.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatePhylogenySynechocystisAllosteric RegulationBacterial ProteinsGlyceric AcidsGlycolysisIsoenzymesKineticsPhosphofructokinasesPhotosynthesisStructure-Activity Relationship3-phosphoglycerateAdenosine DiphosphateAdenosine TriphosphateBacterial ProteinsGlyceric AcidsIsoenzymesPhosphofructokinasesADPADP-dependent PFK-Aallosteric regulationATPcyanobacteriaPFK-A superfamilyPPi signature binding motifs

Identifiers

PMID39393572
PMCPMC11609450

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Registered trials

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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.