Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1928685 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
UMP kinase (PyrH) is an essential enzyme found only in bacteria, making it ideal as a target for the discovery of antibacterials. To identify inhibitors of PyrH, an assay employing Staphylococcus aureus PyrH coupled to pyruvate kinase/lactate dehydrogenase was developed and was used to perform a high throughput screen. A validated aminopyrimidine series was identified from screening. Kinetic characterization of this aminopyrimidine indicated it was a competitive inhibitor of ATP. We have shown that HTS can be used to identify potential leads for this novel target, the first ATP competitive inhibitor of PyrH reported.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Peter Doig, Elise Gorseth, Tory Nash, Arthur Patten, Ning Gao, Carolyn Blackett,