ArticleScientific reports2017
4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 58 citations in OpenAlex.
- Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures.Molecules (Basel, Switzerland) · 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
- 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
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- Metagenomics analysis revealed the distinctive ruminal microbiome and resistive profiles in dairy buffaloes.Animal microbiome · 2021Article
- Shotgun Metagenomics of a Water Kefir Fermentation Ecosystem Reveals a NovelFrontiers in microbiology · 2019Article
- 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
- Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactic acid bacteria possess a diversity of glucansucrase (GS) enzymes that belong to glycoside hydrolase family 70 (GH70) and convert sucrose into α-glucan polysaccharides with (α1 → 2)-, (α1 → 3)-, (α1 → 4)- and/or (α1 → 6)-glycosidic bonds. In recent years 3 novel subfamilies of GH70 enzymes, inactive on sucrose but using maltodextrins/starch as substrates, have been established (e.g. GtfB of Lactobacillus reuteri 121). Compared to the broad linkage specificity found in GSs, all GH70 starch-acting enzymes characterized so far possess 4,6-α-glucanotransferase activity, cleaving (α1 → 4)-linkages and synthesizing new (α1 → 6)-linkages. In this work a gene encoding a putative GH70 family enzyme was identified in the genome of Lactobacillus fermentum NCC 2970, displaying high sequence identity with L. reuteri 121 GtfB 4,6-α-glucanotransferase, but also with unique variations in some substrate-binding residues of GSs. Characterization of this L. fermentum GtfB and its products revealed that it acts as a 4,3-α-glucanotransferase, converting amylose into a new type of α-glucan with alternating (α1 → 3)/(α 1 → 4)-linkages and with (α1 → 3,4) branching points. The discovery of this novel reaction specificity in GH70 family and clan GH-H expands the range of α-glucans that can be synthesized and allows the identification of key positions governing the linkage specificity within the active site of the GtfB-like GH70 subfamily of enzymes.
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