Bioinformatics-facilitated identification of novel bacterial sulfoglycosidases that hydrolyze 6-Sulfo-N-acetylglucosamine

Dong, Mochen, Chen, Zhuoyun, He, Yuan, Zallot, Rémi and Jin, Yi ORCID: https://orcid.org/0000-0002-6927-4371 2024. Bioinformatics-facilitated identification of novel bacterial sulfoglycosidases that hydrolyze 6-Sulfo-N-acetylglucosamine. ACS Bio & Med Chem Au 4 (6) , pp. 342-352. 10.1021/acsbiomedchemau.4c00088

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Abstract

Glycan sulfation is a widespread postglycosylation modification crucial for modulating biological functions including cellular adhesion, signaling, and bacterial colonization. 6-Sulfo-β-GlcNAcases are a class of enzyme that alters sulfation patterns. Such changes in sulfation patterns are linked to diseases such as bowel inflammation, colitis, and cancer. Despite their significance, 6-sulfo-β-GlcNAcases, which cleave β-linked 6-sulfo-N-acetylglucosamine (6S-GlcNAc), have been but rarely identified. This scarcity results mainly from the short, diverse, and distinctive sulfate-binding motifs required for recognition of the 6-sulfate group in 6S-GlcNAc in addition to the conserved GH20 family features. In this study, we discovered 6-sulfo-β-GlcNAcases and assigned two novel sulfate-binding motifs by the use of comparative genomics, structural predictions, and activity-based screening. Our findings expand the known microbiota capable of degrading sulfated glycans and add significant enzymes to the tool kit for analysis and synthesis of sulfated oligosaccharides.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Chemistry
Additional Information:	License information from Publisher: LICENSE 1: URL: https://creativecommons.org/licenses/by/4.0/, Start Date: 2024-11-19
Publisher:	American Chemical Society
ISSN:	2694-2437
Date of First Compliant Deposit:	28 November 2024
Date of Acceptance:	8 November 2024
Last Modified:	15 Jan 2025 14:55
URI:	https://orca.cardiff.ac.uk/id/eprint/174362

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