期刊
COLLECTION OF CZECHOSLOVAK CHEMICAL COMMUNICATIONS
卷 75, 期 12, 页码 1249-1257出版社
INST ORGANIC CHEM AND BIOCHEM
DOI: 10.1135/cccc2010094
关键词
Enzyme inhibitors; Enzyme kinetics; Phosphonates; Purine nucleoside phosphorylase; Phosphates of acyclic nucleoside phosphonates; Tenofovir phosphate congeners
资金
- Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic [Z 40550506]
- Ministry of Education, Youth and Sports of the Czech Republic, v.v.i. [1M0508]
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 K(i) similar to 1.9 x 10(-8) and/or 2.2 x 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 mono-phosphates 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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