Hyaluronidase transglycosylation activity

Table 1 presents a survey of hyaluronidase activity in the venom of several animal species. Transglycosylation properties have been observed with hyaluronidase from snake venom (Crotalus terrificus) [8], but not with hyaluronidase from bee venom [19]. 

The properties of a purified, homogeneous, bovine testicular hyaluronidase (pH optimum 5.0—5.5) have been studied using radiolabelled oligomers of A -acetylhyalobiouronic acid as substrates and acceptors. Transfer of a glycosyl residue to an acceptor occurred with retention of configuration. On the basis of the cleavage and transglycosylation reactions, it was proposed that the active site of the enzyme consists of five subsites that bind disaccharide units. 

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