Structural basis for substrate specificity of mammalian neuraminidases.

ABSTRACT: The removal of sialic acid (Sia) residues from glycoconjugates in vertebrates is mediated by a family of neuraminidases (sialidases) consisting of Neu1, Neu2, Neu3 and Neu4 enzymes. The enzymes play distinct physiological roles, but their ability to discriminate between the types of linkages connecting Sia and adjacent residues and between the identity and arrangement of the underlying sugars has never been systematically studied. Here we analyzed the specificity of neuraminidases by studying the kinetics of hydrolysis of BODIPY-labeled substrates containing common mammalian sialylated oligosaccharides: 3'Sia-LacNAc, 3'SiaLac, SiaLex, SiaLea, SiaLec, 6'SiaLac, and 6'SiaLacNAc. We found significant differences in substrate specificity of the enzymes towards the substrates containing α2,6-li

SUBMITTER: Smutova V 

PROVIDER: S-EPMC4164519 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature