Evidence map›Paper›PMID 26763236›Full record

ArticleThe Journal of biological chemistry2016

Characterization of the First α-(1→3) Branching Sucrases of the GH70 Family.

Marlène Vuillemin, Marion Claverie, Yoann Brison, Etienne Séverac, Pauline Bondy, Sandrine Morel, Pierre Monsan, Claire Moulis, Magali Remaud-Siméon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
7.8field-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

18 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. In Silico Analysis of the Dextransucrase Obtained FromBioinformatics and biology insights · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Unravelling Regioselectivity ofInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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 1 institution in 1 country.

Marlène VuilleminFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Marion ClaverieFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Yoann BrisonFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Etienne SéveracFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Pauline BondyFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Sandrine MorelFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Pierre MonsanFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France.
Claire MoulisFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France moulis@insa-toulouse.fr.
Magali Remaud-SiméonFrom the Université de Toulouse, Institut National des Sciences Appliquées (INSA), Université Paul Sabatié (UPS), Institut National Polytechnique (INP), Laboratoire d'Ingénieries des Systèmes Biologiques et des Procédés (LISBP), 135 Avenue de Rangueil, F-31077 Toulouse, France, CNRS, UMR5504, F-31400 Toulouse, France, and Institut National de la Recherche Agronomique (INRA), UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-3140 Toulouse, France remaud@insa-toulouse.fr.
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leuconostoc citreumNRRL B-742 has been known for years to produce a highly α-(1→3)-branched dextran for which the synthesis had never been elucidated. In this work a gene coding for a putative α-transglucosylase of the GH70 family was identified in the reported genome of this bacteria and functionally characterized. From sucrose alone, the corresponding recombinant protein, named BRS-B, mainly catalyzed sucrose hydrolysis and leucrose synthesis. However, in the presence of sucrose and a dextran acceptor, the enzyme efficiently transferred the glucosyl residue from sucrose to linear α-(1→6) dextrans through the specific formation of α-(1→3) linkages. To date, BRS-B is the first reported α-(1→3) branching sucrase. Using a suitable sucrose/dextran ratio, a comb-like dextran with 50% of α-(1→3) branching was synthesized, suggesting that BRS-B is likely involved in the comb-like dextran produced byL. citreumNRRL B-742. In addition, data mining based on the search for specific sequence motifs allowed the identification of two genes putatively coding for branching sucrases in the genome ofLeuconostoc fallaxKCTC3537 andLactobacillus kunkeeiEFB6. Biochemical characterization of the corresponding recombinant enzymes confirmed their branching specificity, revealing that branching sucrases are not only found inL. citreumspecies. According to phylogenetic analyses, these enzymes are proposed to constitute a new subgroup of the GH70 family.

Indexed as

Bacterial ProteinsSucraseLeuconostocBacterial ProteinsSucrasebranching sucrasecarbohydrateenzymeGH70glucansucraseglucooligosaccharideglycoside hydrolaseglycosylationoligosaccharide

Identifiers

PMID26763236
PMCPMC4817194
OpenAlexW2232885759

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.