ReviewCellular and molecular life sciences : CMLS2016
Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes.
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 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 89 citations in OpenAlex.
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- Do We Still Need Chemistry for Water-Soluble Prodrugs? What Biocatalysis Already Does, and What It Does Not.Pharmaceutics · 2026Review
- 4,6-α-Glucanotransferase: An enzymatic biocatalyst for the modification of starch and starch-food systems.Food chemistry: X · 2026Review
- Genomic diversity, functional differentiation and prophage dynamics in Lactiplantibacillus paraplantarum.NPJ science of food · 2026Article
- Diversity of enzymes for exopolysaccharide synthesis in the fructophilic honeybee symbiont Apilactobacillus kunkeei.BMC microbiology · 2026Article
- Genomic insights into dominant lactic acid bacteria in spoiled plant-based meat analogues.Current research in food science · 2026Article
- Characterization and Monitoring of Isomalto/Malto-Polysaccharide Formation by Different 4,6-α-Glucanotransferases.Journal of agricultural and food chemistry · 2025Article
- Functional role and folding properties of the glucan-binding domain of oral bacterial glucansucrase.FEBS letters · 2025Article
- Screening of 14 Lactic Acid Bacteria for Fermentative Isomalto/Malto-Polysaccharide Synthesis.Journal of agricultural and food chemistry · 2025Article
- Unprecedented Diversity of the Glycoside Hydrolase Family 70: A Comprehensive Analysis of Sequence, Structure, and Function.Journal of agricultural and food chemistry · 2024Article
- The Discovery, Molecular Cloning, and Characterization of DextransucraseMolecules (Basel, Switzerland) · 2024Article
- Stimulus-Responsive Hydrogels as Drug Delivery Systems for Inflammation Targeted Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Analysing the dynamics of the bacterial community in pozol, a Mexican fermented corn dough.Microbiology (Reading, England) · 2023Article
- Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from ThermophilicJournal of agricultural and food chemistry · 2022Article
- The findings of glucosyltransferase enzymes derived from oral streptococci.The Japanese dental science review · 2022Review
- The C-Terminal Domain ofGels (Basel, Switzerland) · 2022Article
- Weaving of bacterial cellulose by the Bcs secretion systems.FEMS microbiology reviews · 2022Review
- Variability of Bacterial Homopolysaccharide Production and Properties during Food Processing.Biology · 2022Review
- Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales.Scientific reports · 2022Article
- Insights into Broad-Specificity Starch Modification from the Crystal Structure ofJournal of agricultural and food chemistry · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactic acid bacteria (LAB) are known to produce large amounts of α-glucan exopolysaccharides. Family GH70 glucansucrase (GS) enzymes catalyze the synthesis of these α-glucans from sucrose. The elucidation of the crystal structures of representative GS enzymes has advanced our understanding of their reaction mechanism, especially structural features determining their linkage specificity. In addition, with the increase of genome sequencing, more and more GS enzymes are identified and characterized. Together, such knowledge may promote the synthesis of α-glucans with desired structures and properties from sucrose. In the meantime, two new GH70 subfamilies (GTFB- and GTFC-like) have been identified as 4,6-α-glucanotransferases (4,6-α-GTs) that represent novel evolutionary intermediates between the family GH13 and "classical GH70 enzymes". These enzymes are not active on sucrose; instead, they use (α1 → 4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize novel α-glucans by introducing linear chains of (α1 → 6) linkages. All these GH70 enzymes are very interesting biocatalysts and hold strong potential for applications in the food, medicine and cosmetic industries. In this review, we summarize the microbiological distribution and the structure-function relationships of family GH70 enzymes, introduce the two newly identified GH70 subfamilies, and discuss evolutionary relationships between family GH70 and GH13 enzymes.
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