Evidence map›Paper›PMID 18848471›Full record

ArticleChemistry & biology2008

Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora.

Tracey M Gloster, Johan P Turkenburg, Jennifer R Potts, Bernard Henrissat, Gideon J Davies

Open access · hybridAbstract read
In one paragraph

Article in Chemistry & biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 109 citations in OpenAlex.

  1. Trial
  2. Degradation of mucinbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Bespoke Activity-Based Probes Reveal that theJournal of the American Chemical Society · 2025
    Article
  5. Article
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  7. Article
  8. Determinants of raffinose family oligosaccharide use inbioRxiv : the preprint server for biology · 2024
    Article
  9. Acarbose Impairs GutbioRxiv : the preprint server for biology · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Three New Acrylic Acid Derivatives fromMolecules (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Tracey M GlosterYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5YW, UK. gloster@ysbl.york.ac.uk
Johan P Turkenburg
Jennifer R Potts
Bernard Henrissat
Gideon J Davies
University of York · GBArchitecture et Fonction des Macromolécules Biologiques · FR

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 082572
6 · The paper itself

Abstract

Enzymatic cleavage of the glycosidic bond yields products in which the anomeric configuration is either retained or inverted. Each mechanism reflects the dispositions of the enzyme functional groups; a facet of which is essentially conserved in 113 glycoside hydrolase (GH) families. We show that family GH97 has diverged significantly, as it contains both inverting and retaining alpha-glycosidases. This reflects evolution of the active center; a glutamate acts as a general base in inverting members, exemplified by Bacteroides thetaiotaomicron alpha-glucosidase BtGH97a, whereas an aspartate likely acts as a nucleophile in retaining members. The structure of BtGH97a and its complexes with inhibitors, coupled to kinetic analysis of active-site variants, reveals an unusual calcium ion dependence. 1H NMR analysis shows an inversion mechanism for BtGH97a, whereas another GH97 enzyme from B. thetaiotaomicron, BtGH97b, functions as a retaining alpha-galactosidase.

Indexed as

Evolution, MolecularBacteroidesBiocatalysisCarbohydrate MetabolismCatalytic DomainEnzyme InhibitorsGlycoside HydrolasesHumansIntestinal MucosaIntestinesKineticsMagnetic Resonance SpectroscopyModels, MolecularProtein Structure, TertiarySequence AnalysisStereoisomerismEnzyme InhibitorsGlycoside Hydrolases

Identifiers

PMID18848471
PMCPMC2670981
OpenAlexW2042112590

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.