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Ground State, Intermediate, and Multivalent Nucleotide Analogue Inhibitors of Cytidine 5′‐Triphosphate Synthase
Author(s) -
Taylor Scott D.,
Lunn Faylene A.,
Bearne Stephen L.
Publication year - 2008
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200800236
Subject(s) - cytidine , nucleotide , atp synthase , nucleotide salvage , chemistry , adenosine triphosphate , biochemistry , enzyme , stereochemistry , gene
CTP synthase (CTPS) catalyzes the conversion of UTP to CTP and is a recognized target for the development of anticancer, antiviral, and antiprotozoal agents. We show that phosphonate and phorphoramidate 5′‐bismethylene triphosphate intermediate analogues 3 – 6 inhibit CTPS activity, as do the multivalent nucleotide inhibitors 7 – 10 . These results support the further development of these two classes of compounds as CTPS inhibitors.

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