Structural basis of α-fucosidase inhibition by iminocyclitols with Ki values in the micro- to picomolar range

Angewandte Chemie - International Edition

Volumn 49, Issue 2, 2010, Pages 337-340

  Wu, Hsing Ju ^a   Ho, Ching Wen ^a,b   Ko, Tzu Ping ^a   Popat, Shinde D ^a   Lin, Chun Hung ^a   Wang, Andrew H J ^a  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

Fucosidases; Iminocyclitols; Inhibitors; Slow binding

Indexed keywords

ACTIVE SITE; CHEMICAL EQUATIONS; CONFORMATIONAL CHANGE; HYDROPHOBIC INTERACTIONS; NANOMOLAR; NANOMOLAR RANGE; STRUCTURAL BASIS;

COMPLEXATION; CONFORMATIONS; HYDROPHOBICITY;

HYDROGEN BONDS;

1 DEOXYNOJIRIMYCIN; ALPHA LEVO FUCOSIDASE; CYCLITOL; ENZYME INHIBITOR;

ARTICLE; BACTERIUM; BINDING SITE; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; HUMAN; KINETICS; PH; STRUCTURE ACTIVITY RELATION; SYNTHESIS; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

1-DEOXYNOJIRIMYCIN; ALPHA-L-FUCOSIDASE; BACTERIA; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYCLITOLS; ENZYME INHIBITORS; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 73349100030     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200905597     Document Type: Article

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34. 1 values are: (5.6 ±0.2), (33.8 ± 2.8), (18.0 ± 0.2), and (53.8 ± 0.9) nM.