title: A 1H NMR investigation of the hydrolysis of a synthetic substrate by KDN-sialidase from Crassostrea virginica.
abstract: The mechanism of hydrolysis of 4-methylumbelliferyl 3-deoxy-D-glycero-alpha-D-galacto-2-nonulopyranosidonic acid (KDN alpha 2MeUmb, 4) by KDN-sialidase isolated from the hepatopancreas of the oyster Crassostrea virginica has been monitored by 1H NMR spectroscopy. The results of these experiments reveal that KDN-sialidase catalyses the hydrolysis of the synthetic substrate KDN alpha 2MeUmb, with initial release of alpha-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 other N-acetylneuraminic acid-recognising sialidases from both viral and bacterial sources.
authors.affiliation: Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Australia.
authors.forename: J C
authors.initials: JC
authors.lastname: Wilson
authors.forename: D C
authors.initials: DC
authors.lastname: Kong
authors.forename: Y T
authors.initials: YT
authors.lastname: Li
authors.forename: M
authors.initials: M
authors.lastname: von Itzstein
mesh_terms: D000818:Animals; D002240:Carbohydrate Sequence; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry / Q000378:metabolism*; D010125:Ostreidae / Q000201:enzymology*; D011522:Protons; D013379:Substrate Specificity; D013400:Sugar Acids / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011522:Protons; D013400:Sugar Acids; C050008:3-deoxyglycero-galacto-nonulosonic acid; D009439:Neuraminidase