Otro
New catalytic mechanism for human purine nucleoside phosphorylase
Registro en:
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 327, n. 3, p. 646-649, 2005.
0006-291X
10.1016/j.bbrc.2004.12.052
WOS:000226674800003
Autor
Canduri, F.
Fadel, V
Basso, L. A.
Palma, Mario Sergio
Santos, D. S.
de Azevedo, W. F.
Resumen
Human purine nucleoside phosphorylase has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Recently, several structures of human PNP have been reported, which allowed redefinition of the active site and understanding of the structural basis for inhibition of PNP by acyclovir and immucillin-H. Based on previously solved human PNP structures, we proposed here a new catalytic mechanism for human PNP, which is supported by crystallographic studies and explains previously determined kinetic data. (C) 2004 Elsevier B.V. All rights reserved.