AI Article Synopsis
- The study investigates the cleavage of the bond between mannose or galactose and amino acids serine or threonine by specific enzymes (alpha-mannosidase and alpha-galactosidase) in glycoproteins.
- Several glycopeptides that mimic the O-glycosyl bond in glycoproteins have been synthesized for experimental analysis.
- The research indicates that cleavage can also take place in glucoamylase following proteolytic degradation of these compounds.
Article Abstract
The possibility of cleavage of the alpha-bond between mannose (or galactose) and serine (or threonine) in the presence of alpha-mannosidase and alpha-galactosidase has been studied. Using model compounds simulating the O-glycosyl bond in glycoproteins, several glycopeptides have been synthesized: N-tertbutyloxycarbonyl-O-alpha-mannopyranosyl-seryl-glycine methylamide (alpha-Man-Ser-Gly), tertbutyl-oxycarbonyl-O-alpha-mannopyranosyl-threonyl- glycine methylamide (alpha-Man-Thr-Gly), N-tertbutyloxy-carbonyl-O-alpha-galactopyranosyl-seryl-glycine methylamide (alpha-Gal-Ser-Gly) as well as N-tertbutyloxy-carbonyl-O-beta-mannopyranosyl-seryl-glycine methylamide (beta-Man-Ser-Gly). The cleavage has been shown to occur in glucoamylase after proteolytic degradation.
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