Conformational Selection of Glycomimetics at Enzyme Catalytic Sites: Experimental Demonstration of the Binding of Distinct High-Energy Distorted Conformations of C-, S-, and O-Gly

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• 作者：Alicia Garc&iacute ; a-Herrero ; Esther Montero ; Jose L. Mu&ntilde ; oz ; Juan F. Espinosa ; Alejandro Viá ; n ; Jose L. Garc&iacute ; a ; Juan L. Asensio ; F. Javier Ca&ntilde ; ada ; and Jesus Jimé ; nez-B
• 刊名：Journal of the American Chemical Society
• 出版年：2002
• 出版时间：May 1, 2002
• 年：2002
• 卷：124
• 期：17
• 页码：4804 - 4810
• 全文大小：167K
• 年卷期：v.124,no.17(May 1, 2002)
• ISSN：1520-5126

文摘

We show that the conformational features of the molecular complexes of E. coli images/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-galactosidaseand O-glycosides may differ from those formed with closely related compounds in their chemical nature,such as C- and S-glycosyl analogues. In the particular case presented here, NMR and ab initio quantummechanical results show that the 3D-shapes of the ligand/inhibitor within the enzyme binding site dependon the chemical nature of the compounds. In fact, they depend on the relative size of the stereoelectronicbariers for chair deformation or for rotation around images/gifchars/Phi.gif" BORDER=0 > glycosidic linkage.