Evidence map›Paper›PMID 39093337›Full record

ArticleThe Biochemical journal2024

Regulation of Rubisco activity by interaction with chloroplast metabolites.

Ana K M Lobo, Douglas J Orr, Elizabete Carmo-Silva

Abstract read
In one paragraph

Article in The Biochemical journal, 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. Photosynthetic Responses to Rising COGlobal change biology · 2026
    Review
  2. Article
  3. Harnessing Setaria as a Model for CPlants (Basel, Switzerland) · 2025
    Review
  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.

Ana K M LoboLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, U.K.ORCID 0000-0002-1471-1327
Douglas J OrrLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, U.K.ORCID 0000-0003-1217-537X
Elizabete Carmo-SilvaLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, U.K.ORCID 0000-0001-6059-9359

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rubisco activity is highly regulated and frequently limits carbon assimilation in crop plants. In the chloroplast, various metabolites can inhibit or modulate Rubisco activity by binding to its catalytic or allosteric sites, but this regulation is complex and still poorly understood. Using rice Rubisco, we characterised the impact of various chloroplast metabolites which could interact with Rubisco and modulate its activity, including photorespiratory intermediates, carbohydrates, amino acids; as well as specific sugar-phosphates known to inhibit Rubisco activity - CABP (2-carboxy-d-arabinitol 1,5-bisphosphate) and CA1P (2-carboxy-d-arabinitol 1-phosphate) through in vitro enzymatic assays and molecular docking analysis. Most metabolites did not directly affect Rubisco in vitro activity under both saturating and limiting concentrations of Rubisco substrates, CO2 and RuBP (ribulose-1,5-bisphosphate). As expected, Rubisco activity was strongly inhibited in the presence of CABP and CA1P. High physiologically relevant concentrations of the carboxylation product 3-PGA (3-phosphoglyceric acid) decreased Rubisco activity by up to 30%. High concentrations of the photosynthetically derived hexose phosphates fructose 6-phosphate (F6P) and glucose 6-phosphate (G6P) slightly reduced Rubisco activity under limiting CO2 and RuBP concentrations. Biochemical measurements of the apparent Vmax and Km for CO2 and RuBP (at atmospheric O2 concentration) and docking interactions analysis suggest that CABP/CA1P and 3-PGA inhibit Rubisco activity by binding tightly and loosely, respectively, to its catalytic sites (i.e. competing with the substrate RuBP). These findings will aid the design and biochemical modelling of new strategies to improve the regulation of Rubisco activity and enhance the efficiency and sustainability of carbon assimilation in rice.

Indexed as

ChloroplastsMolecular Docking SimulationOryzaRibulose-Bisphosphate CarboxylaseCarbon DioxideFructosephosphatesPhotosynthesisPlant ProteinsRibulosephosphatesCarbon Dioxidefructose-6-phosphateFructosephosphatesPlant ProteinsRibulose-Bisphosphate CarboxylaseRibulosephosphatesdocking analysisOryza sativaRubisco inhibitionRubisco regulationstroma metabolites

Identifiers

PMID39093337
PMCPMC11346435

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.