Abstract
The transglycosylation mechanism of testicular hyaluronidase, which is an endo-β- N-acetylhexosaminidase, was investigated with the aim of performing enzymatic synthesis of glycosaminoglycan (GAG) sugar chains. It was found that disaccharide units (glucuronic acid β1-3- N-accetylglucosamine β1-4) are successively released from the nonreducing terminal of a donor hyaluronic acid (HA) and rapidly transferred to the glucuronic acid residue at the nonreducing terminal of an acceptor HA via a β1-4 linkage. By repeating the transglycosylation using suitable combinations of HA, chondroitin (Ch), chondoroitin 4-sulfate (Ch4S), chondroitin 6-sulfate (Ch6S), and desulfate dermatan sulfate (desulfated DS) as acceptors and donors, it was possible to enzymatically synthesize GAG oligosaccharides. As a result, a GAG oligosaccharide library, which has a hybrid structure composed of disaccharide units derived from HA, Ch, Ch4S, Ch6S, and desulfated DS, was prepared. Enzymatically synthesized GAG oligosaccharides show the way to opening new avenues in glycomedicine.
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