ArticleApplied and environmental microbiology2011
4,6-α-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70.
Article in Applied and environmental microbiology, 2011. 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, 95 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
- Article
- 4,6-α-Glucanotransferase: An enzymatic biocatalyst for the modification of starch and starch-food systems.Food chemistry: X · 2026Review
- Characterization and Monitoring of Isomalto/Malto-Polysaccharide Formation by Different 4,6-α-Glucanotransferases.Journal of agricultural and food chemistry · 2025Article
- Screening of 14 Lactic Acid Bacteria for Fermentative Isomalto/Malto-Polysaccharide Synthesis.Journal of agricultural and food chemistry · 2025Article
- Article
- Optimization of 4,6-α and 4,3-α-Glucanotransferase Production inFoods (Basel, Switzerland) · 2024Article
- Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from ThermophilicJournal of agricultural and food chemistry · 2022Article
- Insights into Broad-Specificity Starch Modification from the Crystal Structure ofJournal of agricultural and food chemistry · 2021Article
- Development of Slowly Digestible Starch Derived α-Glucans with 4,6-α-Glucanotransferase and Branching Sucrase Enzymes.Journal of agricultural and food chemistry · 2020Article
- 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
- Mining novel starch-converting Glycoside Hydrolase 70 enzymes from the Nestlé Culture Collection genome database: The Lactobacillus reuteri NCC 2613 GtfB.Scientific reports · 2017Article
- Draft Genome Sequence ofGenome announcements · 2017Article
- 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H.Scientific reports · 2017Article
- Article
- 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
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
- Characterization of the First α-(1→3) Branching Sucrases of the GH70 Family.The Journal of biological chemistry · 2016Article
- The Exiguobacterium sibiricum 255-15 GtfC Enzyme Represents a Novel Glycoside Hydrolase 70 Subfamily of 4,6-α-Glucanotransferase Enzymes.Applied and environmental microbiology · 2016Article
- Amy63, a novel type of marine bacterial multifunctional enzyme possessing amylase, agarase and carrageenase activities.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactobacillus reuteri 121 uses the glucosyltransferase A (GTFA) enzyme to convert sucrose into large amounts of the α-D-glucan reuteran, an exopolysaccharide. Upstream of gtfA lies another putative glucansucrase gene, designated gtfB. Previously, we have shown that the purified recombinant GTFB protein/enzyme is inactive with sucrose. Various homologs of gtfB are present in other Lactobacillus strains, including the L. reuteri type strain, DSM 20016, the genome sequence of which is available. Here we report that GTFB is a novel α-glucanotransferase enzyme with disproportionating (cleaving α1→4 and synthesizing α1→6 and α1→4 glycosidic linkages) and α1→6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates (in short, it is a 4,6-α-glucanotransferase). Characterization of the types of compounds synthesized from maltoheptaose by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), methylation analysis, and 1-dimensional ¹H nuclear magnetic resonance (NMR) spectroscopy revealed that only linear products were made and that with increasing degrees of polymerization (DP), more α1→6 glycosidic linkages were introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB clearly is a member of the glycoside hydrolase 70 (GH70) family, comprising enzymes with a permuted (β/α)₈ barrel that use sucrose to synthesize α-D-glucan polymers. The GTFB enzyme reaction and product specificities, however, are novel for the GH70 family, resembling those of the GH13 α-amylase type of enzymes in using maltooligosaccharides as substrates but differing in introducing a series of α1→6 glycosidic linkages into linear oligosaccharide products. We conclude that GTFB represents a novel evolutionary intermediate between the GH13 and GH70 enzyme families, and we speculate about its origin.
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