Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis.

@article{Wickramasinghe2006KineticIA,
  title={Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis.},
  author={Sasala Roshinie Wickramasinghe and Kirstine A Inglis and Jonathan E Urch and Sylke M{\"u}ller and Daan M F van Aalten and Alan H. Fairlamb},
  journal={The Biochemical journal},
  year={2006},
  volume={393 Pt 2},
  pages={447-57}
}
Type II fatty acid biosynthesis represents an attractive target for the discovery of new antimalarial drugs. Previous studies have identified malarial ENR (enoyl acyl-carrier-protein reductase, or FabI) as the target for the antiseptic triclosan. In the present paper, we report the biochemical properties and 1.5 A (1 A=0.1 nm) crystal structure of OAR (3-oxoacyl acyl-carrier-protein reductase, or FabG), the second reductive step in fatty acid biosynthesis and its inhibition by hexachlorophene… CONTINUE READING