Evidence map›Paper›PMID 16524921›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2006

Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria.

Sacha A F T van Hijum, Slavko Kralj, Lukasz K Ozimek, Lubbert Dijkhuizen, Ineke G H van Geel-Schutten

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

104 citing papers in PubMed, 444 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Fecal Material of Captive Wild Animals as Source of CAZymes With Application Potential.Chembiochem : a European journal of chemical biology · 2026
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  7. AJournal of bacteriology · 2026
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  8. Article
  9. Reproducible 3D bioprinting ofMicrobiology spectrum · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Recent Progress in 1,2-Molecules (Basel, Switzerland) · 2023
    Review
  17. Article
  18. Glycosyltransferases Expression Changes inFoods (Basel, Switzerland) · 2023
    Article
  19. In Situ Raman Analysis of Biofilm Exopolysaccharides Formed inInternational journal of molecular sciences · 2023
    Article
  20. Article

44 more citing papers are in PubMed but not listed here.

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 1 country.

Sacha A F T van HijumDepartment of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands. s.a.f.t.van.hijum@rug.nl
Slavko Kralj
Lukasz K Ozimek
Lubbert Dijkhuizen
Ineke G H van Geel-Schutten
University of Groningen · NLPension Fund for Care and Well-Being · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactic acid bacteria (LAB) employ sucrase-type enzymes to convert sucrose into homopolysaccharides consisting of either glucosyl units (glucans) or fructosyl units (fructans). The enzymes involved are labeled glucansucrases (GS) and fructansucrases (FS), respectively. The available molecular, biochemical, and structural information on sucrase genes and enzymes from various LAB and their fructan and alpha-glucan products is reviewed. The GS and FS enzymes are both glycoside hydrolase enzymes that act on the same substrate (sucrose) and catalyze (retaining) transglycosylation reactions that result in polysaccharide formation, but they possess completely different protein structures. GS enzymes (family GH70) are large multidomain proteins that occur exclusively in LAB. Their catalytic domain displays clear secondary-structure similarity with alpha-amylase enzymes (family GH13), with a predicted permuted (beta/alpha)(8) barrel structure for which detailed structural and mechanistic information is available. Emphasis now is on identification of residues and regions important for GS enzyme activity and product specificity (synthesis of alpha-glucans differing in glycosidic linkage type, degree and type of branching, glucan molecular mass, and solubility). FS enzymes (family GH68) occur in both gram-negative and gram-positive bacteria and synthesize beta-fructan polymers with either beta-(2-->6) (inulin) or beta-(2-->1) (levan) glycosidic bonds. Recently, the first high-resolution three-dimensional structures have become available for FS (levansucrase) proteins, revealing a rare five-bladed beta-propeller structure with a deep, negatively charged central pocket. Although these structures have provided detailed mechanistic insights, the structural features in FS enzymes dictating the synthesis of either beta-(2-->6) or beta-(2-->1) linkages, degree and type of branching, and fructan molecular mass remain to be identified.

Indexed as

Amino Acid SequenceBacterial ProteinsFructansGlycosyltransferasesGram-Positive BacteriaLactic AcidMolecular Sequence DataProtein ConformationStructure-Activity RelationshipSucrasealternansucraseBacterial ProteinsFructansGlycosyltransferasesLactic AcidSucrase

Identifiers

PMID16524921
PMCPMC1393251
OpenAlexW2111051779

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.