Sialidase-2 Protein, Mouse (P.pastoris, His)

Sialidase-2 is an exo-alpha-sialidase that catalyzes the hydrolytic cleavage of terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) during the catabolism of glycolipids, glycoproteins, and oligosaccharides. It recognizes the sialyl linkage positions of the glycan moiety as well as the supramolecular organization of sialoglycoconjugates (By similarity). The enzyme shows a preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric and micellar forms. It exclusively hydrolyzes monomeric GM1 ganglioside but exhibits no activity toward the micellar form (By similarity). Sialidase-2 displays lower sialidase activity for glycoproteins like fetuin and transferrin, which carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages (By similarity). It cleaves the milk oligosaccharide alpha-(2->3)-sialyllactose but is inactive toward the alpha-(2->6)-sialyllactose isomer and colominic acid, a homopolymer of alpha-(2->8)-linked Neu5Ac residues (By similarity).