Ndeh, Didier, Rogowski, Artur, Cartmell, Alan, Luis, Ana S., Baslé, Arnaud, Gray, Joseph, Venditto, Immacolata, Briggs, Jonathon, Zhang, Xiaoyang, Labourel, Aurore, Terrapon, Nicolas, Buffetto, Fanny, Nepogodiev, Sergey, Xiao, Yao, Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275, Zhu, Yanping, O'Neill, Malcolm A., Urbanowicz, Breeanna R., York, William S., Davies, Gideon J., Abbott, D. Wade, Ralet, Marie Christine, Martens, Eric C., Henrissat, Bernard and Gilbert, Harry J. (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature, 544 (7648). pp. 65-70. ISSN 0028-0836
Full text not available from this repository. (Request a copy)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.
Item Type: | Article |
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Additional Information: | Publisher Copyright: © 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. |
Uncontrolled Keywords: | general ,/dk/atira/pure/subjectarea/asjc/1000 |
Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology |
Related URLs: | |
Depositing User: | LivePure Connector |
Date Deposited: | 04 Sep 2024 12:33 |
Last Modified: | 25 Sep 2024 18:06 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/96518 |
DOI: | 10.1038/nature21725 |
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