Evidence map›Paper›PMID 27141938›Full record

ReviewCellular and molecular life sciences : CMLS2016

GH13 amylosucrases and GH70 branching sucrases, atypical enzymes in their respective families.

Claire Moulis, Isabelle André, Magali Remaud-Simeon

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

21 citing papers in PubMed, 58 citations in OpenAlex.

  1. Fecal Material of Captive Wild Animals as Source of CAZymes With Application Potential.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Review
  3. Enzymatic Glycosylation ofBiomolecules · 2025
    Review
  4. Review
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  7. Article
  8. Article
  9. Review
  10. Article
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  12. Article
  13. Review
  14. Uridine Diphosphate-Dependent Glycosyltransferases fromInternational journal of molecular sciences · 2018
    Article
  15. 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

3 authors at 3 institutions in 1 country.

Claire MoulisUniversité de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077, Toulouse, France.
Isabelle AndréUniversité de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077, Toulouse, France.
Magali Remaud-SimeonUniversité de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077, Toulouse, France. remaud@insa-toulouse.fr.
Centre National de la Recherche Scientifique · FRLaboratoire d'Ingénierie des Systèmes Biologiques et des Procédés · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylosucrases and branching sucrases are α-retaining transglucosylases found in the glycoside-hydrolase families 13 and 70, respectively, of the clan GH-H. These enzymes display unique activities in their respective families. Using sucrose as substrate and without mediation of nucleotide-activated sugars, amylosucrase catalyzes the formation of an α-(1 → 4) linked glucan that resembles amylose. In contrast, the recently discovered branching sucrases are unable to catalyze polymerization of glucosyl units as they are rather specific for dextran branching through α-(1 → 2) or α-(1 → 3) branching linkages depending on the enzyme regiospecificity. In addition, GH13 amylosucrases and GH70 branching sucrases are naturally promiscuous and can glucosylate different types of acceptor molecules including sugars, polyols, or flavonoids. Amylosucrases have been the most investigated glucansucrases, in particular to control product profiles or to successfully develop tailored α-transglucosylases able to glucosylate various molecules of interest, for example, chemically protected carbohydrates that are planned to enter in chemoenzymatic pathways. The structural traits of these atypical enzymes will be described and compared, and an overview of the potential of natural or engineered enzymes for glycodiversification and chemoenzymatic synthesis will be highlighted.

Indexed as

Multigene FamilyAmino Acid SequenceGlucosyltransferasesGlycosyltransferasesKineticsModels, MolecularProtein EngineeringalternansucraseamylosucraseGlucosyltransferasesGlycosyltransferasesAmylosucraseBranching sucrase glucansucraseSucrose-active enzymesTransglucosylation

Identifiers

PMID27141938
PMCPMC11108324
OpenAlexW2346832518

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.