Uses
O-Glycosidase is used to release the Gal-β(1,3)-GaINAc unit from
O-glycans (glycoproteins or glycopeptides). Bindings to serine as well as to threonine are hydrolyzed. Substituents at the disaccharide (
e.g., sialic acid) prevent the hydrolysis and, therefore, have to be removed chemically or enzymatically (
e.g., with neuraminidase from
Arthrobacter or from
Vibrio cholerae).
O-Glycosidase has been used to selectively deglycosylated chondroitin sulfate proteoglycans (CSPGs).
General Description
O-Glycan-peptide hydrolase
O-Glycopeptide endo-D-galactosyl-N-acetyl-α-galactosamino hydrolase
O-Glycosidase is isolated from the culture filtrate of
Diplococcus pneumoniae
Biochem/physiol Actions
Releases unsubstituted Ser- and Thr-linked β-Gal-(1→3)-α-GalNAc (Core 1 type O-glycan) from glycoproteins. Substitutions of the disaccharide core with sialic acid, lactosamine (galactose-N-acetyl glucosamine), or fucose will block hydrolysis and prevent the liberation of the oligosaccharide from the protein. Pretreament with glycolytic enzymes to remove substituent saccharides from the O-glycan may be needed prior to cleavage using O-glycosidase..
