Design and synthesis of 2'-deoxy-2'-fluorodisaccharides as mechanism- based glycosidase inhibitors that exploit aglycon specificity

Journal of the American Chemical Society

Volumn 119, Issue 25, 1997, Pages 5792-5797

  McCarter, John D ^a   Yeung, Wai ^a   Chow, Jack ^a   Dolphin, David ^a   Withers, Stephen G ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSIDASE; CELLOBIOSE; DISACCHARIDE; FLUORODEOXYGLUCOSE; GLUCOSYLCERAMIDASE; GLUCOSYLCERAMIDE; GLYCOSIDASE; GLYCOSIDASE INHIBITOR;

ARTICLE; CARBOHYDRATE ANALYSIS; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; RHIZOBIUM; SYNTHESIS;

EID: 0030787909     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9627454     Document Type: Article

References (16)

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6. 18
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9. a ≈ 14).
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13. 4.13 using inactivator concentrations of 0.57, 1.30, 2.60, 4.90, 9.80, and 20.00 mM.
14. Street, I. P.; Kempton, J. B.; Withers, S. G. Biochemistry 1992, 31, 9970.
15. 19 The ester bond between inhibitor and peptide is one of the more labile bonds present, undergoing homolytic cleavage with loss of a neutral sugar. The two quadrupoles are scanned in a linked mode so that only those ions differing by the mass of the label could be detected. For a singly-charged peptide, the m/z difference is the mass of the label (165); for a doubly-charged peptide, the m/z difference is half of the mass of the label, and so on. See refs 19 and 20.
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