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Structure and Function of Mammalian Sialidases

  • Eugenio Monti
  • Taeko MiyagiEmail author
Chapter
Part of the Topics in Current Chemistry book series (TOPCURRCHEM, volume 366)

Abstract

The removal of sialic acids, catalyzed by sialidase, is the initial step in degradation of oligosaccharides, glycoproteins, and glycolipids. The catalytic reaction may greatly influence biological processes through changing the conformation of glycoproteins and create or mask binding sites of functional molecules. Recent progress in sialidase research has clarified that mammalian sialidases indeed contribute to the regulation of various cellular functions as well as lysosomal catabolism, unlike the sialidases of microbial origin that probably play roles limited to nutrition and pathogenesis. However, the mammalian enzymes contain consensus sequences in the six-blade β-propeller structural organization typical of microbial sialidases, despite the low degree of similarity to the amino acid sequences of the microbial enzymes. The present review briefly summarizes structural and functional features of mammalian sialidases.

Keywords

Ganglioside Glycoprotein Sialic acid Sialidase Transmembrane signaling 

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Copyright information

© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  1. 1.Faculty of Medicine, Department of Biomedical Sciences and BiotechnologyUniversity of Brescia, BresciaBresciaItaly
  2. 2.Division of Cancer Glycosylation Research, Institute of Molecular Biomembrane and GlycobiologyTohoku Pharmaceutical UniversitySendaiJapan

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