Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.

@article{Moche1999StructureOT,
  title={Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.},
  author={Martin Moche and G. R. Eugenia Schneider and Patricia Edwards and Katayoon Dehesh and Ylva Lindqvist},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 10},
  pages={6031-4}
}
In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein (ACP) synthases catalyze chain elongation by the addition of two-carbon units derived from malonyl-ACP to an acyl group bound to either ACP or CoA. The enzyme is a possible drug target for treatment of certain cancers and for tuberculosis. The crystal structure of the complex of the enzyme from Escherichia coli, and the fungal mycotoxin cerulenin reveals that the inhibitor is bound in a hydrophobic pocket formed at the… CONTINUE READING

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