Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10771449 | Biochemical and Biophysical Research Communications | 2005 | 4 Pages |
Abstract
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.
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Authors
Fernanda Canduri, Valmir Fadel, Luiz Augusto Basso, Mário Sérgio Palma, Diógenes Santiago Santos, Walter Filgueira Jr.,