Discovery of an Allosteric Inhibitor Binding Site in 3-Oxo-acyl-ACP Reductase from Pseudomonas aeruginosa

@inproceedings{Cukier2013DiscoveryOA,
  title={Discovery of an Allosteric Inhibitor Binding Site
in 3-Oxo-acyl-ACP Reductase from Pseudomonas aeruginosa},
  author={Cyprian D. Cukier and Anthony G. Hope and Ayssar A. Elamin and Lucile Moyni{\'e} and Robert Schnell and Susanne Schach and Holger Kneuper and Mahavir Singh and James H. Naismith and Ylva Lindqvist and David W Gray and G. R. Eugenia Schneider},
  booktitle={ACS chemical biology},
  year={2013}
}
3-Oxo-acyl-acyl carrier protein (ACP) reductase (FabG) plays a key role in the bacterial fatty acid synthesis II system in pathogenic microorganisms, which has been recognized as a potential drug target. FabG catalyzes reduction of a 3-oxo-acyl-ACP intermediate during the elongation cycle of fatty acid biosynthesis. Here, we report gene deletion experiments that support the essentiality of this gene in P. aeruginosa and the identification of a number of small molecule FabG inhibitors with IC50… CONTINUE READING
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