Evidence map›Paper›PMID 38758412›Full record

ArticlePlant molecular biology2024

Pyruvate kinase 2 from Synechocystis sp. PCC 6803 increased substrate affinity via glucose-6-phosphate and ribose-5-phosphate for phosphoenolpyruvate consumption.

Masahiro Karikomi, Noriaki Katayama, Takashi Osanai

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Plant molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. A conserved peptidase governs glucose homeostasis inbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. 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

3 authors.

Masahiro KarikomiSchool of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan.
Noriaki KatayamaSchool of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan.
Takashi OsanaiSchool of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan. tosanai@meiji.ac.jp.ORCID http://orcid.org/0000-0003-2229-6028

Funding

Japan Science and Technology Corporation JPMJAL1306Japan Society for the Promotion of Science 20H02905
6 · The paper itself

Abstract

Pyruvate kinase (Pyk, EC 2.7.1.40) is a glycolytic enzyme that generates pyruvate and adenosine triphosphate (ATP) from phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP), respectively. Pyk couples pyruvate and tricarboxylic acid metabolisms. Synechocystis sp. PCC 6803 possesses two pyk genes (encoded pyk1, sll0587 and pyk2, sll1275). A previous study suggested that pyk2 and not pyk1 is essential for cell viability; however, its biochemical analysis is yet to be performed. Herein, we biochemically analyzed Synechocystis Pyk2 (hereafter, SyPyk2). The optimum pH and temperature of SyPyk2 were 7.0 and 55 °C, respectively, and the K

Indexed as

Glucose-6-PhosphatePhosphoenolpyruvatePyruvate KinaseRibosemonophosphatesSynechocystisBacterial ProteinsHydrogen-Ion ConcentrationKineticsSubstrate SpecificityTemperatureBacterial ProteinsGlucose-6-PhosphatePhosphoenolpyruvatePyruvate Kinaseribose-5-phosphateRibosemonophosphatesGlycolysisMicroalgaePyruvate kinaseSynechocystis sp. PCC 6803

Identifiers

PMID38758412
PMCPMC11101554

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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.