Biochemistry and Function of Sialidases

  • Megumi Saito
  • Robert K. Yu


Sialidases (EC; N-acylneuraminosyl glycohydrolase) are a family of exoglycosidases that catalyze the cleavage of nonreducing sialic acid residues ketosidically linked to mono-or oligosaccharide chains of glycoconjugates. They are widely distributed in viruses, bacteria, fungi, mycoplasma, and protozoa as well as avian and mammalian species (Rosenberg and Schengrund, 1976; Corfield et al., 1981a; Corfield and Schauer, 1982; Conzelmann and Sandhoff, 1987; Corfield, 1992). Among the various sialidase species, viral and bacterial enzymes have been studied extensively; a number of them have been purified to homogeneity and characterized for their properties and structures. Mammalian sialidases are more labile and often are bound tightly to membranes, hindering successful purification of these enzymes. Much attention, however, has been directed toward these enzymes as interest in the metabolism and biological function of sialoglycoconjugates in mammalian cells has grown in recent years (Schauer, 1982, 1985, 1991; Ledeen, 1989; Schengrund, 1990; Varki, 1992). The term “sialidase” was first proposed by Heimer and Meyer (1956), and “neuraminidase” was introduced a year later (Gottschalk, 1957). Both names have been used interchangeably in the literature. Since the enzyme does not usually apply to neuraminic acid itself, but to its derivatives, sialic acid, the term “sialidase” is deemed more appropriate (Rosenberg and Schengrund, 1976).


Influenza Virus Sialic Acid Newcastle Disease Virus Clostridium Perfringens Trypanosoma Cruzi 
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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Megumi Saito
    • 1
  • Robert K. Yu
    • 1
  1. 1.Department of Biochemistry and Molecular Biophysics, Medical College of VirginiaVirginia Commonwealth UniversityRichmondUSA

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