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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/ISPT_STRPN ISPT_STRPN] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | | [https://www.uniprot.org/uniprot/ISPT_STRPN ISPT_STRPN] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Undecaprenyl pyrophosphate synthase (UppS) is an essential enzyme in bacterial cell wall synthesis. Here we report the discovery of Staphylococcus aureus UppS inhibitors from an Encoded Library Technology screen and demonstrate binding to the hydrophobic substrate site through cocrystallography studies. The use of bacterial strains with regulated uppS expression and inhibitor resistant mutant studies confirmed that the whole cell activity was the result of UppS inhibition, validating UppS as a druggable antibacterial target.
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| Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase.,Concha N, Huang J, Bai X, Benowitz A, Brady P, Grady LC, Kryn LH, Holmes D, Ingraham K, Jin Q, Pothier Kaushansky L, McCloskey L, Messer JA, O'Keefe H, Patel A, Satz AL, Sinnamon RH, Schneck J, Skinner SR, Summerfield J, Taylor A, Taylor JD, Evindar G, Stavenger RA J Med Chem. 2016 Jul 20. PMID:27379833<ref>PMID:27379833</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5kh2" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]] | | *[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
