Evidence map›Paper›PMID 23601637›Full record

ArticleChemistry & biology2013

Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria.

Farzana Miah, Hendrik Koliwer-Brandl, Martin Rejzek, Robert A Field, Rainer Kalscheuer, Stephen Bornemann

Abstract read
In one paragraph

Article in Chemistry & biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Exquisite specificity of Pks13 defines the essentiality of trehalose in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. TargetingACS infectious diseases · 2024
    Article
  4. Review
  5. Article
  6. Synthesis of CFrontiers in chemistry · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Tailoring Trehalose for Biomedical and Biotechnological Applications.Pure and applied chemistry. Chimie pure et appliquee · 2017
    Article
  15. Article
  16. Article
  17. Review
  18. Free Trehalose Accumulation in DormantFrontiers in microbiology · 2017
    Article
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Farzana MiahDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich, Norfolk NR4 7UH, UK.
Hendrik Koliwer-Brandl
Martin Rejzek
Robert A Field
Rainer Kalscheuer
Stephen Bornemann
John Innes Centre · GBHeinrich Heine University Düsseldorf · DE

Funding

Biotechnology and Biological Sciences Research Council BB/F017294/1Biotechnology and Biological Sciences Research Council BB/J004561/1Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618Biotechnology and Biological Sciences Research Council BBS/E/J/000C0647
6 · The paper itself

Abstract

Trehalose synthase (TreS) was thought to catalyze flux from maltose to trehalose, a precursor of essential trehalose mycolates in mycobacterial cell walls. However, we now show, using a genetic approach, that TreS is not required for trehalose biosynthesis in Mycobacterium smegmatis, whereas two alternative trehalose-biosynthetic pathways (OtsAB and TreYZ) are crucial. Consistent with this direction of flux, trehalose levels in Mycobacterium tuberculosis decreased when TreS was overexpressed. In addition, TreS was shown to interconvert the α anomer of maltose and trehalose using (1)H and (19)F-nuclear magnetic resonance spectroscopies using its normal substrates and deoxyfluoromaltose analogs, with the nonenzymatic mutarotation of α/β-maltose being slow. Therefore, flux through TreS in mycobacteria flows from trehalose to α-maltose, which is the appropriate anomer for maltose kinase of the GlgE α-glucan pathway, which in turn contributes to intracellular and/or capsular polysaccharide biosynthesis.

Indexed as

Cell WallGlucosyltransferasesMagnetic Resonance SpectroscopyMaltoseMycobacterium smegmatisMycobacterium tuberculosisPhosphoric Monoester HydrolasesTrehaloseGlucosyltransferasesMaltosePhosphoric Monoester HydrolasesTrehalosetrehalose-6-phosphate synthasetrehalose synthase

Identifiers

PMID23601637
PMCPMC3918855
OpenAlexW2012089496

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.