A1H NMR investigation of the hydrolysis of a synthetic substrate by KDN-sialidase fromCrassostrea virginica
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- Wilson, J.C., Kong, D.C.M., Li, YT. et al. Glycoconjugate J (1996) 13: 927. doi:10.1007/BF01053187
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The mechanism of hydrolysis of 4-methylumbelliferyl 3-deoxy-d-glycero-α-d-galacto-2-nonulopyranosidonic acid (KDNα2MeUmb,4) by KDN-sialidase isolated from the hepatopancreas of the oysterCrassostrea virginica has been monitored by1H NMR spectroscopy. The results of these experiments reveal that KDN-sialidase catalyses the hydrolysis of the synthetic substrate KDNα2MeUmb, with initial release of α-d-KDN. This is consistent with an overall mechanism for the hydrolysis which proceeds with retention of anomeric configuration. These results agree with earlier NMR studies of otherN-acetylneuraminic acid-recognising sialidases from both viral and bacterial sources.