Abstract
Several C-1 homologated GlcNAc- and GalNAc-thiazolines, as well as a related GalNAc-thiazole, have been prepared. The compounds are analogues of GlcNAc-thiazoline, a potent transition-state-mimicking inhibitor of retaining beta-N-acetylglycosaminidases. Kinetic evaluation of these fused pyranose-heterocycles against the bacterial N-acetylhexosaminidase SpHex suggests active site steric restrictions around the substrate anomeric carbon.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Carbohydrate Sequence
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Carbon / chemistry
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / pharmacology*
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Galactose / chemical synthesis
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Galactose / pharmacology*
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Glucosamine / analogs & derivatives*
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Glucosamine / chemical synthesis
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Glucosamine / pharmacology
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Kinetics
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Models, Chemical
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Molecular Sequence Data
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Piperidines / chemistry
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Piperidines / pharmacology
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Substrate Specificity
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Thiazoles / chemical synthesis
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Thiazoles / pharmacology*
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beta-N-Acetylhexosaminidases / antagonists & inhibitors*
Substances
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Enzyme Inhibitors
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GlcNAc-thiazoline
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Piperidines
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Thiazoles
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Carbon
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beta-N-Acetylhexosaminidases
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Glucosamine
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Galactose