ArticleThe Journal of biological chemistry2016
Structural Insights into the Carbohydrate Binding Ability of an α-(1→2) Branching Sucrase from Glycoside Hydrolase Family 70.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The trial behind it
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- One-step enzymatic synthesis of medium molecular weight dextran using engineered dextransucrase DarM fromFrontiers in microbiology · 2026Article
- Unprecedented Diversity of the Glycoside Hydrolase Family 70: A Comprehensive Analysis of Sequence, Structure, and Function.Journal of agricultural and food chemistry · 2024Article
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- A specific oligosaccharide-binding site in the alternansucrase catalytic domain mediates alternan elongation.The Journal of biological chemistry · 2020Article
- Processivity of dextransucrases synthesizing very-high-molar-mass dextran is mediated by sugar-binding pockets in domain V.The Journal of biological chemistry · 2020Article
- Alleviating the Hydrolysis of Carbohydrates, Tangzhiqing (TZQ) Decreased the Postprandial Glycemia in Healthy Volunteers: An Eight-Period Crossover Study.Evidence-based complementary and alternative medicine : eCAM · 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
- Combining multi-scale modelling methods to decipher molecular motions of a branching sucrase from glycoside-hydrolase family 70.PloS one · 2018Article
- Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives.Molecules (Basel, Switzerland) · 2016Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The α-(1→2) branching sucrase ΔN123-GBD-CD2 is a transglucosylase belonging to glycoside hydrolase family 70 (GH70) that catalyzes the transfer ofd-glucosyl units from sucroseto dextrans or gluco-oligosaccharides via the formation of α-(1→2) glucosidic linkages. The first structures of ΔN123-GBD-CD2 in complex withd-glucose, isomaltosyl, or isomaltotriosyl residues were solved. The glucose complex revealed three glucose-binding sites in the catalytic gorge and six additional binding sites at the surface of domains B, IV, and V. Soaking with isomaltotriose or gluco-oligosaccharides led to structures in which isomaltosyl or isomaltotriosyl residues were found in glucan binding pockets located in domain V. One aromatic residue is systematically identified at the bottom of these pockets in stacking interaction with one glucosyl moiety. The carbohydrate is also maintained by a network of hydrogen bonds and van der Waals interactions. The sequence of these binding pockets is conserved and repeatedly present in domain V of several GH70 glucansucrases known to bind α-glucans. These findings provide the first structural evidence of the molecular interaction occurring between isomalto-oligosaccharides and domain V of the GH70 enzymes.
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Registered trials
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