Bioinformatics-Facilitated Identification of Novel Bacterial Sulfoglycosidases That Hydrolyze 6-Sulfo-N-acetylglucosamine.

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-bin

SUBMITTER: Dong M 

PROVIDER: S-EPMC11659886 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature