ArticleApplied and environmental microbiology2002
Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1-->4) and alpha-(1-->6) glucosidic bonds.
Article in Applied and environmental microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 122 citations in OpenAlex.
- Glucansucrases as versatile biocatalysts: structural insights, synthesis of emerging prebiotic oligosaccharides, and their functional roles in food matrices.Antonie van Leeuwenhoek · 2026Review
- Evaluating microbial regulation as a preventive strategy for radiation-related caries: A review.Head & face medicine · 2025Review
- Fermentation of Orange Peels by Lactic Acid Bacteria: Impact on Phenolic Composition and Antioxidant Activity.Foods (Basel, Switzerland) · 2024Article
- Characterization of Dextran Biosynthesized by Glucansucrase fromAntioxidants (Basel, Switzerland) · 2023Article
- Host specific adaptations ofCurrent research in microbial sciences · 2023Article
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- Lactobacilli and human dental caries: more than mechanical retention.Microbiology (Reading, England) · 2022Article
- Isolation, Characterization and Biosafety Evaluation of Lactobacillus Fermentum OK with Potential Oral Probiotic Properties.Probiotics and antimicrobial proteins · 2021Article
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes.Applied and environmental microbiology · 2018Article
- Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri.Applied microbiology and biotechnology · 2017Article
- 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H.Scientific reports · 2017Article
- Enhanced Probiotic Potential ofFrontiers in microbiology · 2017Article
- Structural determinants of alternating (α1 → 4) and (α1 → 6) linkage specificity in reuteransucrase of Lactobacillus reuteri.Scientific reports · 2016Article
- Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- The pan-genome of Lactobacillus reuteri strains originating from the pig gastrointestinal tract.BMC genomics · 2015Article
- Structure and biosynthesis of two exopolysaccharides produced by Lactobacillus johnsonii FI9785.The Journal of biological chemistry · 2013Article
- 4,6-α-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily.Applied microbiology and biotechnology · 2013Article
- Article
- 4,6-α-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70.Applied and environmental microbiology · 2011Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactobacillus reuteri strain 121 produces a unique, highly branched, soluble glucan in which the majority of the linkages are of the alpha-(1-->4) glucosidic type. The glucan also contains alpha-(1-->6)-linked glucosyl units and 4,6-disubstituted alpha-glucosyl units at the branching points. Using degenerate primers, based on the amino acid sequences of conserved regions from known glucosyltransferase (gtf) genes from lactic acid bacteria, the L. reuteri strain 121 glucosyltransferase gene (gtfA) was isolated. The gtfA open reading frame (ORF) was 5,343 bp, and it encodes a protein of 1,781 amino acids with a deduced M(r) of 198,637. The deduced amino acid sequence of GTFA revealed clear similarities with other glucosyltransferases. GTFA has a relatively large variable N-terminal domain (702 amino acids) with five unique repeats and a relatively short C-terminal domain (267 amino acids). The gtfA gene was expressed in Escherichia coli, yielding an active GTFA enzyme. With respect to binding type and size distribution, the recombinant GTFA enzyme and the L. reuteri strain 121 culture supernatants synthesized identical glucan polymers. Furthermore, the deduced amino acid sequence of the gtfA ORF and the N-terminal amino acid sequence of the glucosyltransferase isolated from culture supernatants of L. reuteri strain 121 were the same. GTFA is thus responsible for the synthesis of the unique glucan polymer in L. reuteri strain 121. This is the first report on the molecular characterization of a glucosyltransferase from a Lactobacillus strain.
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