Evidence map›Paper›PMID 22923411›Full record

ArticleApplied and environmental microbiology2012

Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont.

M Cervera-Tison, L E Tailford, C Fuell, L Bruel, G Sulzenbacher, B Henrissat, J G Berrin, M Fons, T Giardina, N Juge

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2012. 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
3.9field-weighted citation impact, top 7% 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, 56 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Complete Genome Analysis ofMicroorganisms · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Sucrose 6Microbial genomics · 2019
    Article
  13. Article
  14. Review
  15. Fecal microbiota in pouchitis and ulcerative colitis.World journal of gastroenterology · 2016
    Article
  16. Article
  17. Article
  18. 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

10 authors at 5 institutions in 2 countries.

M Cervera-TisonInstitute of Food Research, The Gut Health and Food Safety Institute Strategic Programme, Norwich Research Park, Norwich, United Kingdom.
L E Tailford
C Fuell
L Bruel
G Sulzenbacher
B Henrissat
J G Berrin
M Fons
T Giardina
N Juge
Quadram Institute · GBAix-Marseille Université · FRCentre National de la Recherche Scientifique · FRArchitecture et Fonction des Macromolécules Biologiques · FRInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FR

Funding

Biotechnology and Biological Sciences Research Council BBS/E/F/00044452Biotechnology and Biological Sciences Research Council IFR/08/1
6 · The paper itself

Abstract

Ruminococcus gnavus belongs to the 57 most common species present in 90% of individuals. Previously, we identified an α-galactosidase (Aga1) belonging to glycoside hydrolase (GH) family 36 from R. gnavus E1 (M. Aguilera, H. Rakotoarivonina, A. Brutus, T. Giardina, G. Simon, and M. Fons, Res. Microbiol. 163:14-21, 2012). Here, we identified a novel GH36-encoding gene from the same strain and termed it aga2. Although aga1 showed a very simple genetic organization, aga2 is part of an operon of unique structure, including genes putatively encoding a regulator, a GH13, two phosphotransferase system (PTS) sequences, and a GH32, probably involved in extracellular and intracellular sucrose assimilation. The 727-amino-acid (aa) deduced Aga2 protein shares approximately 45% identity with Aga1. Both Aga1 and Aga2 expressed in Escherichia coli showed strict specificity for α-linked galactose. Both enzymes were active on natural substrates such as melibiose, raffinose, and stachyose. Aga1 and Aga2 occurred as homotetramers in solution, as shown by analytical ultracentrifugation. Modeling of Aga1 and Aga2 identified key amino acids which may be involved in substrate specificity and stabilization of the α-linked galactoside substrates within the active site. Furthermore, Aga1 and Aga2 were both able to perform transglycosylation reactions with α-(1,6) regioselectivity, leading to the formation of product structures up to [Hex](12) and [Hex](8), respectively. We suggest that Aga1 and Aga2 play essential roles in the metabolism of dietary oligosaccharides and could be used for the design of galacto-oligosaccharide (GOS) prebiotics, known to selectively modulate the beneficial gut microbiota.

Indexed as

alpha-GalactosidaseAmino Acid SequenceAnimalsGastrointestinal TractGlycosylationMelibioseMolecular Sequence DataOligosaccharidesProtein Structure, TertiaryRaffinoseRatsRuminococcusSequence AlignmentSequence Analysis, ProteinSubstrate Specificityalpha-GalactosidaseMelibioseOligosaccharidesRaffinosestachyose

Identifiers

PMID22923411
PMCPMC3485720
OpenAlexW2140843850

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.