Evidence map›Paper›PMID 18326043›Full record

ArticleThe Journal of biological chemistry2008

A novel GDP-dependent pyruvate kinase isozyme from Toxoplasma gondii localizes to both the apicoplast and the mitochondrion.

Tomoya Saito, Manami Nishi, Muoy I Lim, Bo Wu, Takuya Maeda, Hisayuki Hashimoto, Tsutomu Takeuchi, David S Roos, Takashi Asai

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 52 citations in OpenAlex.

  1. Engineering riboflavin-overproducingSynthetic and systems biotechnology · 2026
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  7. An overview of structure, function, and regulation of pyruvate kinases.Protein science : a publication of the Protein Society · 2019
    Review
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  11. Journal of lipid research · 2018
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  20. Rewiring and regulation of cross-compartmentalized metabolism in protists.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Review
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

9 authors at 3 institutions in 2 countries.

Tomoya SaitoDepartment of Tropical Medicine and Parasitology, Keio University School of Medicine, 35 Shinanomachi, Tokyo 160-8582, Japan. asait@sc.itc.keio.ac.jp
Manami Nishi
Muoy I Lim
Bo Wu
Takuya Maeda
Hisayuki Hashimoto
Tsutomu Takeuchi
David S Roos
Takashi Asai
University of Pennsylvania · USKeio University · JPKeio University Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported a cytosolic pyruvate kinase (EC 2.7.1.40) from Toxoplasma gondii (TgPyKI) that differs from most eukaryotic pyruvate kinases in being regulated by glucose 6-phosphate rather than fructose 1,6-diphosphate. Another putative pyruvate kinase (TgPyKII) was identified from parasite genome, which exhibits 32% amino acid sequence identity to TgPyKI and retains pyruvate kinase signature motifs and amino acids essential for substrate binding and catalysis. Whereas TgPyKI is most closely related to plant/algal enzymes, phylogenetic analysis suggests a proteobacterial origin for TgPyKII. Enzymatic characterization of recombinant TgPyKII shows a high pH optimum at 8.5, and a preference for GDP as a phosphate recipient. Catalytic activity is independent of K+, and no allosteric or regulatory effects were observed in the presence of fructose 1,6-diphosphate, fructose 2,6-diphosphate, glucose 6-phosphate, ribose 5-phosphate, AMP, or ATP. Unlike TgPyKI, native TgPyKII activity was exclusively associated with the membranous fraction of a T. gondii tachyzoite lysate. TgPyKII possesses a long N-terminal extension containing five putative start codons before the conserved region and localizes to both apicoplast and mitochondrion by immunofluorescence assay using native antibody and fluorescent protein fusion to the N-terminal extension. Further deletional and site-directed mutagenesis suggests that a translation product from 1st Met is responsible for the localization to the apicoplast, whereas one from 3rd Met is for the mitochondrion. This is the first study of a potential mitochondrial pyruvate kinase in any system.

Indexed as

Amino Acid SequenceAnimalsGuanosine DiphosphateKineticsMitochondriaModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedPhylogenyProtein BindingProtein IsoformsPyruvate KinaseRecombinant ProteinsSequence Homology, Amino AcidToxoplasmaGuanosine DiphosphateProtein IsoformsPyruvate KinaseRecombinant Proteins

Identifiers

PMID18326043
PMCPMC2376232
OpenAlexW1991515156

What OpenQuestion holds

Textmetadata
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.