Ndeh, Didier, Rogowski, Artur, Cartmell, Alan et al. (22 more authors) (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. pp. 65-70. ISSN 0028-0836
Abstract
The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron uses the most structurally complex glycan known: The plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017, Macmillan Publishers Limited, part of Springer Nature. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Keywords: | Bacteroides thetaiotaomicron/enzymology,Biocatalysis,Borates/chemistry,Catalytic Domain,Gastrointestinal Microbiome,Gastrointestinal Tract/microbiology,Glycoside Hydrolases/chemistry,Humans,Models, Molecular,Pectins/chemistry,Substrate Specificity |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 03 May 2017 13:40 |
Last Modified: | 19 Feb 2025 17:00 |
Published Version: | https://doi.org/10.1038/nature21725 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1038/nature21725 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:115950 |
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