Progress in Structure, Function and Catalytic Reactions of Sialidase and Sialyltransferase

Sialidase and sialyltransferase play important roles in various biological and pathological processes. Generally, sialidase has the ability to cleave the glycosidic bond of terminal sialic acid to hydrolyze sialoglycoconjugates, and sialyltransferase can use CMP-Neu5Ac as substrate to transfer sialyl group to a new glycosyl acceptor. In this paper, the family, structure, function, especially the catalytic reactions of sialidase and sialyltransferase are reviewed. The assay of the enzymes is briefly introduced. The future developing prospects of sialidase and sialyltransferase are also discussed.