Abstract
Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 α-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Biocatalysis
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Catalytic Domain
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Clostridium perfringens / enzymology*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / metabolism*
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Imidazoles / chemistry
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Imidazoles / metabolism*
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Mannose / analogs & derivatives
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Mannose / metabolism*
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Molecular Conformation
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Mutation
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Protein Binding
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alpha-Mannosidase / chemistry
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alpha-Mannosidase / genetics
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alpha-Mannosidase / metabolism*
Substances
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Enzyme Inhibitors
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Imidazoles
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alpha-Mannosidase
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Mannose