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Updated: Jun 2, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
Features and applications of bacterial sialidases
Seonghun Kim1, Doo-Byoung Oh, Hyun Ah Kang
1Microbe-based Fusion Technology Research Center, Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, 181 Ipsin-gil, Jeongeup, South Korea.
Bacterial sialidases (glycosyl hydrolases) exhibit diverse substrate specificities for cleaving and transferring sialic acids. These enzymes offer potential for synthesizing complex glycans and analyzing glycan structures.
Area of Science:
- Biochemistry
- Glycobiology
- Enzymology
Background:
- Sialidases (neuraminidases) are glycosyl hydrolases releasing terminal N-acylneuraminate residues from glycans.
- Bacterial sialidases utilize sialic acids as nutrients or recognize host cell surface glycans.
- Despite structural similarities, bacterial sialidases display varied biochemical properties, including linkage and substrate specificities.
Purpose of the Study:
- To review the biochemical features of bacterial sialidases.
- To discuss their applications in regioselective hydrolysis and transglycosylation for synthesizing complex glycans.
Main Methods:
- Literature review of bacterial sialidase properties and applications.
- Analysis of enzymatic mechanisms including hydrolysis and transglycosylation.
- Discussion of chemoenzymatic synthesis and glycan structure analysis.
Main Results:
- Bacterial sialidases hydrolyze sialic acids linked via α(2,3)-, α(2,6)-, or α(2,8)-linkages.
- Some sialidases catalyze transglycosylation, transferring sialic acids to asialoglycoconjugates.
- Enzyme specificities vary widely among different bacterial sialidases.
Conclusions:
- Bacterial sialidases possess diverse catalytic capabilities, including hydrolysis and transglycosylation.
- These enzymes are valuable tools for chemoenzymatic synthesis of complex sialylated glycans.
- Understanding bacterial sialidase specificity aids in glycan structure analysis and therapeutic applications.
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