ChemInform Abstract: Powerful Probes for Glycosidases: Novel, Fluorescently Tagged Glycosidase Inhibitors.

Hermetter, Albin; Scholze, Hubert; Stuetz, A. E.; Withers, Stephen G.; Wrodnigg, Tanja

doi:10.1002/chin.200137199

Cited by 1 publication

(2 citation statements)

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“…Isofagomine (2) has a nitrogen atom at the "anomeric" position and is a strong inhibitor of -glucosidase [22][23][24][25][26][27]. The five-membered compound dihydroxymethyl dihydroxypyrrolidine (DMDP, 4), which lacks a 2-OH group, is a potent inhibitor of -glucosidase [28][29][30][31][32][33][34][35][36][37]. A DMDP analogue (5) lacking one of the hydroxymethyl groups also exhibits inhibitory activity againstglucosidase [30,33,36,[38][39][40][41][42].…”

Section: Inhibitors Of Glucosidasesmentioning

confidence: 98%

“…The C5-methyl compound 135 is an inhibitor of fucosidase [42,78,103,120], while the C2-acetamido compound 150 is an inhibitor of -N-acetylglucosaminidase [31]. The latter's parent compound 151 carrying an amino functional group was transformed into a variety of compounds as candidate inhibitors of -glucosidase, from which a compound 171 having a coumarin-type moiety was found to be a very potent inhibitor (Ki 1.2 nM) [34,35].…”

Section: Trans-diol (I-typementioning

confidence: 99%

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3,4-Dihydroxypyrrolidine as Glycosidase Inhibitor

Suzuki

Nakahara²,

Kanie³

2009

CTMC

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Glycosidases are involved in various important biological processes including digestion of starch in the intestine, oligosaccharide processing inside rough ER and Golgi apparatus, and degradation of glycoconjugates in lysosomes. It is apparent that inhibitors of this class of enzymes are useful in the investigation of biological functions of glycoconjugates. Furthermore, it is believed that these compounds are important as pharmaceuticals. The structures of glycosidase inhibitors can be categorized into two major classes; ground-state mimetics and transition-state mimetics. The former has a chair-shaped six-membered structure that mimics monosaccharides where ring oxygens are often replaced with other elements for an improved binding affinity. On the other hand, the latter possesses a somewhat distorted shape compared with the chair conformation of carbohydrates. One of the ways to derive such distortion is by the introduction of sp2 character into the six-membered ring, and another is by ring contraction to form a five-membered system for the transition-state mimetics. The functions of these transition-state mimetics are often unpredictable regarding inhibitory activity and enzyme specificity. This review focuses on such "difficult to predict" species in an attempt to extract information or common aspects for the future development of inhibitors of glycosidases based on transition-state mimetics.

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