Handbook of Glycosyltransferases and Related Genes pp 1047-1052 | Cite as
Uronyl 2-O-sulfotransferase is a class of enzyme that transfers a sulfo group to the 2-OH position of glucuronic acid (GlcA) or iduronic acid (IdoA) present in chondroitin sulfate polysaccharides. Two closely related 2-O-sulfotransferases have been reported: heparan sulfate 2-O-sulfotransferase (HS2ST) (Kobayashi et al. 1997) and chondroitin uronyl 2-O-sulfotransferase (CS2ST) (Kobayashi et al. 1999). CS2ST specifically sulfates CS substrates that consist of the disaccharide repeating unit of GlcA (or) IdoA linked to a galactosamine residue (Fig. 93.1a), whereas HS2ST sulfates only HS substrates that consist of the disaccharide unit of GlcA (or) IdoA linked to a glucosamine residue (Fig. 93.1b). CS2ST and HS2ST share about 56 % homology in the sulfotransferase domain. The products resulting from HS2ST and CS2ST contain 2-O-sulfated glucuronic acid (GlcA2S) and 2-O-sulfated iduronic acid (IdoA2S) residues. The biological functions of IdoA2S residues present in HS have been implicated in binding to fibroblast growth factors to promote cell growth (Bai 1996; Wang et al. 2010; Xu et al. 2012). However, the biological functions of IdoA2S residues present in CS are less defined. This chapter is primarily focused on the discovery of CS2ST (Kobayashi et al. 1999) and a recent mutagenesis study in CS2ST (Xu et al. 2007).
KeywordsGlucuronic Acid Dermatan Sulfate Sulfo Group Iduronic Acid Sulfotransferase Activity
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