A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer

The atomic-resolution structure of a xylobiose-derived isofagomine lactam in complex with the xylanase Xyn10A from Streptomyces lividans reveals that the lactam is bound to the enzyme as the amide tautomer, with "reversed" protonation-states for nucleophile and acid-base.

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2003-04 (8), p.944-945
Main Authors: Gloster, Tracey, Williams, Spencer J, Tarling, Chris A, Roberts, Shirley, Dupont, Claude, Jodoin, Pascalé, Shareck, François, Withers, Stephen G, Davies, Gideon J
Format: Article
Language:English
Subjects:
Amides - chemistry
Binding, Competitive
Crystallography, X-Ray
Disaccharides - chemistry
Disaccharides - metabolism
Disaccharides - pharmacology
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - metabolism
Enzyme Inhibitors - pharmacology
Glycoside Hydrolases - antagonists & inhibitors
Glycoside Hydrolases - metabolism
Imino Pyranoses
Lactams - chemistry
Lactams - metabolism
Lactams - pharmacology
Models, Molecular
Piperidines - chemistry
Piperidines - metabolism
Piperidines - pharmacology
Streptomyces - enzymology
Xylan Endo-1,3-beta-Xylosidase
Xylosidases - metabolism
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Description
Summary:The atomic-resolution structure of a xylobiose-derived isofagomine lactam in complex with the xylanase Xyn10A from Streptomyces lividans reveals that the lactam is bound to the enzyme as the amide tautomer, with "reversed" protonation-states for nucleophile and acid-base.
ISSN:1359-7345
DOI:10.1039/b301829f