Recent advances on glycosyltransferases involved in the biosynthesis of the proteoglycan linkage region

Proteoglycans (PGs) are an essential family of glycoproteins, which can play roles in many important biological events including cell proliferation, cancer development, and pathogen infections. Proteoglycans consist of a core protein with one or multiple glycosaminoglycan (GAG) chains, which are covalently attached to serine residues of serine-glycine dipeptide within the core protein through a common tetrasaccharide linkage. In the past three decades, four key glycosyl transferases involved in the biosynthesis of PG linkage have been discovered and investigated. This review aims to provide an overview on progress made on these four enzymes, with foci on enzyme expression/purification, substrate specificity, activity determination, product characterization, and structure-activity relationship analysis.