Evidence map›Paper›PMID 22676716›Full record

ArticleMolecular microbiology2012

Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase.

Giulia Bandini, Karina Mariño, M Lucia Sampaio Güther, Amy K Wernimont, Sabine Kuettel, Wei Qiu, Shamshad Afzal, Anna Kelner, Raymond Hui, Michael A J Ferguson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  11. CRISPR/Cas9 and glycomics tools forThe Journal of biological chemistry · 2019
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  13. Single-subunit oligosaccharyltransferases ofThe Journal of biological chemistry · 2017
    Article
  14. Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Advances in protein chemistry and structural biology · 2017
    Article
  15. Article
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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 4 countries.

Giulia BandiniDivision of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Karina Mariño
M Lucia Sampaio Güther
Amy K Wernimont
Sabine Kuettel
Wei Qiu
Shamshad Afzal
Anna Kelner
Raymond Hui
Michael A J Ferguson
University of Dundee · GBStructural Genomics Consortium · CANational Institute for Bioprocessing Research and Training · IE

Funding

Wellcome Trust 085622
6 · The paper itself

Abstract

The enzymes phosphomannomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase (PGM) reversibly catalyse the transfer of phosphate between the C6 and C1 hydroxyl groups of mannose, N-acetylglucosamine and glucose respectively. Although genes for a candidate PMM and a PAGM enzymes have been found in the Trypanosoma brucei genome, there is, surprisingly, no candidate gene for PGM. The TbPMM and TbPAGM genes were cloned and expressed in Escherichia coli and the TbPMM enzyme was crystallized and its structure solved at 1.85 Å resolution. Antibodies to the recombinant proteins localized endogenous TbPMM to glycosomes in the bloodstream form of the parasite, while TbPAGM localized to both the cytosol and glycosomes. Both recombinant enzymes were able to interconvert glucose-phosphates, as well as acting on their own definitive substrates. Analysis of sugar nucleotide levels in parasites with TbPMM or TbPAGM knocked down by RNA interference (RNAi) suggests that, in vivo, PGM activity is catalysed by both enzymes. This is the first example in any organism of PGM activity being completely replaced in this way and it explains why, uniquely, T. brucei has been able to lose its PGM gene. The RNAi data for TbPMM also showed that this is an essential gene for parasite growth.

Indexed as

AcetylglucosamineAmino Acid MotifsAmino Acid SequenceGlucose-6-PhosphateGlucosephosphatesKineticsMannosephosphatesModels, MolecularMolecular Sequence DataOpen Reading FramesPhosphoglucomutasePhosphotransferases (Phosphomutases)Protein ConformationProtein TransportRecombinant ProteinsRNA InterferenceAcetylglucosamineglucose-1-phosphateGlucose-6-PhosphateGlucosephosphatesMannosephosphatesN-acetylglucosamine-1-phosphatePhosphoglucomutasephosphomannomutasePhosphotransferases (Phosphomutases)Recombinant Proteins

Identifiers

PMID22676716
PMCPMC3465800
OpenAlexW1911092773

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.