ArticleThe Journal of biological chemistry2014
Evidence that GH115 α-glucuronidase activity, which is required to degrade plant biomass, is dependent on conformational flexibility.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Novel GH115 xylan α-1,2-glucuronidases with distinct preferences for xylan-derived oligomers and polymers.Protein science : a publication of the Protein Society · 2026Article
- Fluorogenic, Subsingle-Turnover Monitoring of Enzymatic Reactions Involving NAD(P)H Provides a Generalized Platform for Directed Ultrahigh-Throughput Evolution of Biocatalysts in Microdroplets.Journal of the American Chemical Society · 2025Article
- Use of xylosidase 3C from Segatella baroniae to discriminate xylan non-reducing terminus substitution characteristics.BMC research notes · 2024Article
- Grass xylan structural variation suggests functional specialization and distinctive interaction with cellulose and lignin.The Plant journal : for cell and molecular biology · 2023Article
- Enzymatic debranching is a key determinant of the xylan-degrading activity of family AA9 lytic polysaccharide monooxygenases.Biotechnology for biofuels and bioproducts · 2023Article
- A GH115 α-glucuronidase structure reveals dimerization-mediated substrate binding and a proton wire potentially important for catalysis.Acta crystallographica. Section D, Structural biology · 2022Article
- PUL-Mediated Plant Cell Wall Polysaccharide Utilization in the Gut Bacteroidetes.International journal of molecular sciences · 2021Review
- The coordinated action of glucuronoyl esterase and α-glucuronidase promotes the disassembly of lignin-carbohydrate complexes.FEBS letters · 2021Article
- BdGT43B2 functions in xylan biosynthesis and is essential for seedling survival inPlant direct · 2020Article
- A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.World journal of microbiology & biotechnology · 2019Review
- Development of an oligosaccharide library to characterise the structural variation in glucuronoarabinoxylan in the cell walls of vegetative tissues in grasses.Biotechnology for biofuels · 2019Article
- Identification of an algal xylan synthase indicates that there is functional orthology between algal and plant cell wall biosynthesis.The New phytologist · 2018Article
- Temporal Expression Dynamics of Plant Biomass-Degrading Enzymes by a Synthetic Bacterial Consortium Growing on Sugarcane Bagasse.Frontiers in microbiology · 2018Article
- Structural Characterization of Mannan Cell Wall Polysaccharides in Plants Using PACE.Journal of visualized experiments : JoVE · 2017Article
- Unusual active site location and catalytic apparatus in a glycoside hydrolase family.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Removal of glucuronic acid from xylan is a strategy to improve the conversion of plant biomass to sugars for bioenergy.Biotechnology for biofuels · 2017Article
- Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T.The Journal of biological chemistry · 2016Article
- The two Rasamsonia emersonii α-glucuronidases, ReGH67 and ReGH115, show a different mode-of-action towards glucuronoxylan and glucuronoxylo-oligosaccharides.Biotechnology for biofuels · 2016Article
- A GH115 α-glucuronidase from Schizophyllum commune contributes to the synergistic enzymatic deconstruction of softwood glucuronoarabinoxylan.Biotechnology for biofuels · 2016Article
- Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors.
Funding
Abstract
The microbial degradation of the plant cell wall is an important biological process that is highly relevant to environmentally significant industries such as the bioenergy and biorefining sectors. A major component of the wall is glucuronoxylan, a β1,4-linked xylose polysaccharide that is decorated with α-linked glucuronic and/or methylglucuronic acid (GlcA/MeGlcA). Recently three members of a glycoside hydrolase family, GH115, were shown to hydrolyze MeGlcA side chains from the internal regions of xylan, an activity that has not previously been described. Here we show that a dominant member of the human microbiota, Bacteroides ovatus, contains a GH115 enzyme, BoAgu115A, which displays glucuronoxylan α-(4-O-methyl)-glucuronidase activity. The enzyme is significantly more active against substrates in which the xylose decorated with GlcA/MeGlcA is flanked by one or more xylose residues. The crystal structure of BoAgu115A revealed a four-domain protein in which the active site, comprising a pocket that abuts a cleft-like structure, is housed in the second domain that adopts a TIM barrel-fold. The third domain, a five-helical bundle, and the C-terminal β-sandwich domain make inter-chain contacts leading to protein dimerization. Informed by the structure of the enzyme in complex with GlcA in its open ring form, in conjunction with mutagenesis studies, the potential substrate binding and catalytically significant amino acids were identified. Based on the catalytic importance of residues located on a highly flexible loop, the enzyme is required to undergo a substantial conformational change to form a productive Michaelis complex with glucuronoxylan.
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