Features and applications of bacterial sialidases = 세균 시알리다아제의 특성과 응용

Cited 54 time in scopus
Metadata Downloads
Features and applications of bacterial sialidases = 세균 시알리다아제의 특성과 응용
Seong Hun KimDoo-Byoung Oh; H A Kang; Oh Suk Kwon
Bibliographic Citation
Applied Microbiology and Biotechnology, vol. 91, no. 1, pp. 1-15
Publication Year
Sialidases, or neuraminidases (EC, 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.
Chemoenzymatic synthesisIn vitro trans-sialylationRegioselectivitySialic acidSialidaseSialoglycoconjugate
Appears in Collections:
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Aging Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.