Evidence map›Paper›PMID 26246447›Full record

ArticlePlant physiology2015

GLYCOLATE OXIDASE3, a Glycolate Oxidase Homolog of Yeast l-Lactate Cytochrome c Oxidoreductase, Supports l-Lactate Oxidation in Roots of Arabidopsis.

Martin K M Engqvist, Jessica Schmitz, Anke Gertzmann, Alexandra Florian, Nils Jaspert, Muhammad Arif, Salma Balazadeh, Bernd Mueller-Roeber, Alisdair R Fernie, Veronica G Maurino

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 50 citations in OpenAlex.

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  7. Scrutinizing the Impact of Alternating Electromagnetic Fields on Molecular Features of the Model PlantInternational journal of environmental research and public health · 2022
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  8. DspA/E-Triggered Non-Host Resistance againstInternational journal of molecular sciences · 2022
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  19. Review
  20. 2-Hydroxy Acids in Plant Metabolism.The arabidopsis book · 2015
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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

10 authors at 3 institutions in 1 country.

Martin K M EngqvistInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).ORCID http://orcid.org/0000-0003-2174-2225
Jessica SchmitzInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).
Anke GertzmannInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).
Alexandra FlorianInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).
Nils JaspertInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).
Muhammad ArifInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).ORCID http://orcid.org/0000-0002-2429-1899
Salma BalazadehInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).ORCID http://orcid.org/0000-0002-5789-4071
Bernd Mueller-RoeberInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).ORCID http://orcid.org/0000-0002-1410-464X
Alisdair R FernieInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.).
Veronica G MaurinoInstitute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences, 40225 Duesseldorf, Germany (M.K.M.E., J.S., A.G., N.J., V.G.M.);Max-Planck-Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany (A.F., A.R.F.); andInstitute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany (M.A., S.B., B.M.-R.) veronica.maurino@uni-duesseldorf.de.ORCID http://orcid.org/0000-0002-3124-1451
Max Planck Society · DEMax Planck Institute of Molecular Plant Physiology · DECluster of Excellence on Plant Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In roots of Arabidopsis (Arabidopsis thaliana), l-lactate is generated by the reduction of pyruvate via l-lactate dehydrogenase, but this enzyme does not efficiently catalyze the reverse reaction. Here, we identify the Arabidopsis glycolate oxidase (GOX) paralogs GOX1, GOX2, and GOX3 as putative l-lactate-metabolizing enzymes based on their homology to CYB2, the l-lactate cytochrome c oxidoreductase from the yeast Saccharomyces cerevisiae. We found that GOX3 uses l-lactate with a similar efficiency to glycolate; in contrast, the photorespiratory isoforms GOX1 and GOX2, which share similar enzymatic properties, use glycolate with much higher efficiencies than l-lactate. The key factor making GOX3 more efficient with l-lactate than GOX1 and GOX2 is a 5- to 10-fold lower Km for the substrate. Consequently, only GOX3 can efficiently metabolize l-lactate at low intracellular concentrations. Isotope tracer experiments as well as substrate toxicity tests using GOX3 loss-of-function and overexpressor plants indicate that l-lactate is metabolized in vivo by GOX3. Moreover, GOX3 rescues the lethal growth phenotype of a yeast strain lacking CYB2, which cannot grow on l-lactate as a sole carbon source. GOX3 is predominantly present in roots and mature to aging leaves but is largely absent from young photosynthetic leaves, indicating that it plays a role predominantly in heterotrophic rather than autotrophic tissues, at least under standard growth conditions. In roots of plants grown under normoxic conditions, loss of function of GOX3 induces metabolic rearrangements that mirror wild-type responses under hypoxia. Thus, we identified GOX3 as the enzyme that metabolizes l-lactate to pyruvate in vivo and hypothesize that it may ensure the sustainment of low levels of l-lactate after its formation under normoxia.

Indexed as

Alcohol OxidoreductasesArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantGenetic Complementation TestGlycolatesLactic AcidL-Lactate Dehydrogenase (Cytochrome)MutationOxidation-ReductionPlant RootsPlants, Genetically ModifiedSaccharomyces cerevisiaeSequence Homology, Amino AcidSubstrate SpecificityAlcohol OxidoreductasesArabidopsis ProteinsGlycolatesglycolic acidglycollate oxidaseGox1 protein, ArabidopsisGox3 protein, ArabidopsisLactic AcidL-Lactate Dehydrogenase (Cytochrome)

Identifiers

PMID26246447
PMCPMC4587471
OpenAlexW2102472706

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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.