Yang, Xiaohong and Yang, Xiaoxiao and Yu, Hai and Na, Lan and Ghosh, Tamashree and McArthur, John B. and Chou, Tsui-Fen and Dickson, Patricia and Chen, Xi (2021) A GH89 human α-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. AMB Express, 11 . Art. No. 94. ISSN 2191-0855. PMCID PMC8225759. doi:10.1186/s13568-021-01253-1. https://resolver.caltech.edu/CaltechAUTHORS:20210630-194140069
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Abstract
Carbohydrate-Active enZYme (CAZY) GH89 family enzymes catalyze the cleavage of terminal α-N-acetylglucosamine from glycans and glycoconjugates. Although structurally and mechanistically similar to the human lysosomal α-N-acetylglucosaminidase (hNAGLU) in GH89 which is involved in the degradation of heparan sulfate in the lysosome, the reported bacterial GH89 enzymes characterized so far have no or low activity toward α-N-acetylglucosamine-terminated heparosan oligosaccharides, the preferred substrates of hNAGLU. We cloned and expressed several soluble and active recombinant bacterial GH89 enzymes in Escherichia coli. Among these enzymes, a truncated recombinant α-N-acetylglucosaminidase from gut symbiotic bacterium Bacteroides thetaiotaomicron ∆22Bt3590 was found to catalyze the cleavage of the terminal α1–4-linked N-acetylglucosamine (GlcNAc) from a heparosan disaccharide with high efficiency. Heparosan oligosaccharides with lengths up to decasaccharide were also suitable substrates. This bacterial α-N-acetylglucosaminidase could be a useful catalyst for heparan sulfate analysis.
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| Additional Information: | © The Author(s) 2021. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. Received 07 June 2021; Accepted 15 June 2021; Published 24 June 2021. This work was financially supported in part by the United States (US) National Institutes of Health (NIH) Grant Number U01GM125288 (to HY) and Million Dollar Bike Ride Grant Program form the Orphan Disease Center in the University of Pennsylvania (to PD). Availability of data and materials: All data generated or analyzed during this study are included in this published article. Ethics approval and consent to participation: Not applicable. Consent for publication: Not applicable. The authors declare no competing interests. | |||||||||
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| Subject Keywords: | α-N-Acetylglucosaminidase; NAGLU; Bacterial glycoside hydrolases; Heparosan oligosaccharides; Bacteroides thetaiotaomicron | |||||||||
| PubMed Central ID: | PMC8225759 | |||||||||
| DOI: | 10.1186/s13568-021-01253-1 | |||||||||
| Record Number: | CaltechAUTHORS:20210630-194140069 | |||||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20210630-194140069 | |||||||||
| Official Citation: | Yang, X., Yang, X., Yu, H. et al. A GH89 human α-N-acetylglucosaminidase (hNAGLU) homologue from gut microbe Bacteroides thetaiotaomicron capable of hydrolyzing heparosan oligosaccharides. AMB Expr 11, 94 (2021). https://doi.org/10.1186/s13568-021-01253-1 | |||||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
| ID Code: | 109679 | |||||||||
| Collection: | CaltechAUTHORS | |||||||||
| Deposited By: | Tony Diaz | |||||||||
| Deposited On: | 02 Jul 2021 20:35 | |||||||||
| Last Modified: | 12 Jul 2021 15:01 |
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