scholarly journals Structure-Activity Relationships for a Collection of Structurally Diverse Inhibitors of Purine Nucleoside Phosphorylase.

2001 ◽  
Vol 49 (1) ◽  
pp. 10-17 ◽  
Author(s):  
Adriano D. ANDRICOPULO ◽  
Rosendo A. YUNES
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Structure Activity Relationships ◽  
Structure Activity

Structure−Activity Relationships for a Class of Inhibitors of Purine Nucleoside Phosphorylase

1999 ◽  
Vol 42 (13) ◽  
pp. 2422-2431 ◽  
Author(s):  
Victor Farutin ◽  
Lori Masterson ◽  
Adriano D. Andricopulo ◽  
Jianming Cheng ◽  
Brad Riley ◽  
...  
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Structure Activity Relationships ◽  
Structure Activity

Inhibition of human purine nucleoside phosphorylase by tenofovir phosphate congeners

2010 ◽  
Vol 75 (12) ◽  
pp. 1249-1257 ◽  
Author(s):  
Ivan Votruba ◽  
Jana Trýznová ◽  
Petra Břehová ◽  
Eva Tloušťová ◽  
Květoslava Horská ◽  
...  
Keyword(s):  
Mixed Type ◽  
Purine Nucleoside Phosphorylase ◽  
Docking Studies ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Purine Bases ◽  
Structure Activity ◽  
Derivatives Of

The structure-activity study on the phosphates of phosphonomethoxypropyl derivatives of purine bases interacting with human purine nucleoside phosphorylase has shown that the most efficient inhibitors of the enzyme are (R)- and (S)-PMPGp with Ki ~ 1.9 × 10–8 and/or 2.2 × 10–8 mol/l. The kinetic experiments have proven, with the exception of both enantiomers of PMP-8-BrDAPp, strictly competitive character of inhibition for all ANP monophosphates tested. Bromine derivatives exhibited uncompetitive and mixed type of inhibition as well. These results were confirmed by docking studies. The substitution of purine moiety with the bromine at the position 8 lead to an allosteric binding of these compounds toward the enzyme.

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