ArticleScientific reports2017
Mechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans.
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 13 papers.
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13 citing papers in PubMed.
- A β-1,2-glucan-associated glycoside hydrolase family 1 β-glucosidase from Streptomyces griseus.Protein science : a publication of the Protein Society · 2025Article
- New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025Article
- Enzymes that catalyze cyclization of β-1,2-glucans.Applied microbiology and biotechnology · 2025Review
- Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens.Nature communications · 2024Article
- Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.Applied microbiology and biotechnology · 2024Article
- Insights to improve the activity of glycosyl phosphorylases from RuminococcusFrontiers in chemistry · 2023Article
- Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022Review
- β-Glucan phosphorylases in carbohydrate synthesis.Applied microbiology and biotechnology · 2021Review
- Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution.Synthetic and systems biotechnology · 2021Article
- Article
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Structural and thermodynamic insights into β-1,2-glucooligosaccharide capture by a solute-binding protein inThe Journal of biological chemistry · 2018Article
- Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis.Carbohydrate research · 2017Article
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11 authors.
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Abstract
Glycoside phosphorylases catalyze the phosphorolysis of oligosaccharides into sugar phosphates. Recently, we found a novel phosphorylase acting on β-1,2-glucooligosaccharides with degrees of polymerization of 3 or more (1,2-β-oligoglucan phosphorylase, SOGP) in glycoside hydrolase family (GH) 94. Here, we characterized SOGP from Lachnoclostridium phytofermentans (LpSOGP) and determined its crystal structure. LpSOGP is a monomeric enzyme that contains a unique β-sandwich domain (Ndom1) at its N-terminus. Unlike the dimeric GH94 enzymes possessing catalytic pockets at their dimer interface, LpSOGP has a catalytic pocket between Ndom1 and the catalytic domain. In the complex structure of LpSOGP with sophorose, sophorose binds at subsites +1 to +2. Notably, the Glc moiety at subsite +1 is flipped compared with the corresponding ligands in other GH94 enzymes. This inversion suggests the great distortion of the glycosidic bond between subsites -1 and +1, which is likely unfavorable for substrate binding. Compensation for this disadvantage at subsite +2 can be accounted for by the small distortion of the glycosidic bond in the sophorose molecule. Therefore, the binding mode at subsites +1 and +2 defines the substrate specificity of LpSOGP, which provides mechanistic insights into the substrate specificity of a phosphorylase acting on β-1,2-glucooligosaccharides.
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