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Title 

Features and applications of bacterial sialidases

 

세균 시알리다아제의 특성과 응용

Authors 

Seong Hun KimDoo-Byoung OhH A KangOh Suk Kwon

Publisher 

Springer Verlag (Germany)

Issue Date 

2011

Citation 

Applied Microbiology and Biotechnology, vol. 91, no. 1, pp. 1-15

Keywords 

Chemoenzymatic synthesisIn vitro trans-sialylationRegioselectivitySialic acidSialidaseSialoglycoconjugate

Abstract 

Sialidases, or neuraminidases (EC 3.2.1.18), belong to a class of glycosyl hydrolases that release terminal N-acylneuraminate residues from the glycans of glycoproteins, glycolipids, and polysaccharides. In bacteria, sialidases can be used to scavenge sialic acids as a nutrient from various sialylated substrates or to recognize sialic acids exposed on the surface of the host cell. Despite the fact that bacterial sialidases share many structural features, their biochemical properties, especially their linkage and substrate specificities, vary widely. Bacterial sialidases can catalyze the hydrolysis of terminal sialic acids linked by the α(2,3)-, α(2,6)-, or α(2,8)-linkage to a diverse range of substrates. In addition, some of these enzymes can catalyze the transfer of sialic acids from sialoglycans to asialoglycoconjugates via a transglycosylation reaction mechanism. Thus, some bacterial sialidases have been applied to synthesize complex sialyloligosaccharides through chemoenzymatic approaches and to analyze the glycan structure. In this review article, the biochemical features of bacterial sialidases and their potential applications in regioselective hydrolysis reactions as well as sialylation by transglycosylation for the synthesis of sialylated complex glycans are discussed.

ISSN 

0175-7598

Link 

http://dx.doi.org/10.1007/s00253-011-3307-2

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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