Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation.

@article{Lindsey1995InhibitionOM,
  title={Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation.},
  author={Stephen Lindsey and H. James Harwood},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 16},
  pages={9083-96}
}
Squalene synthetase (SQS, EC 2.5.1.21) catalyzes the first committed step in the formation of cholesterol and thus represents an ideal site for selectively inhibiting sterol formation. Previous studies have demonstrated that the fungal metabolite, zaragozic acid A (ZGA-A), inhibits SQS activity by mimicking the substrate farnesyl pyrophosphate, the reaction intermediate presqualene pyrophosphate, or both, through a process that confers increased apparent potency in the presence of reduced… CONTINUE READING