Flight of a cytidine deaminase complex with an imperfect transition state analogue inhibitor: Mass spectrometric evidence for the presence of a trapped water molecule
GK Schroeder, L Zhou, MJ Snider, X Chen…
文献索引：Schroeder, Gottfried K.; Zhou, Li; Snider, Mark J.; Chen, Xian; Wolfenden, Richard Biochemistry, 2012 , vol. 51, # 32 p. 6476 - 6486
Cytidine deaminase (CDA) binds the inhibitor zebularine as its 3, 4-hydrate (K d∼ 10–12 M), capturing all but∼ 5.6 kcal/mol of the free energy of binding expected of an ideal transition state analogue (K tx∼ 10–16 M). On the basis of its entropic origin, that shortfall was tentatively ascribed to the trapping of a water molecule in the enzyme–inhibitor complex, as had been observed earlier for product uridine [Snider, MJ, and Wolfenden, R. ...
