Hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase.

@article{Li2007HepaticCP,
  title={Hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase.},
  author={Li Li and T. D. Porter},
  journal={Archives of biochemistry and biophysics},
  year={2007},
  volume={461 1},
  pages={76-84}
}
Squalene monooxygenase is a microsomal enzyme that catalyzes the conversion of squalene to 2,3(s)-oxidosqualene, the immediate precursor to lanosterol in the cholesterol biosynthesis pathway. Unlike other flavoprotein monooxygenases that obtain electrons directly from NAD(P)H, squalene monooxygenase requires a redox partner, and for many years it has been assumed that NADPH-cytochrome P450 reductase is this requisite redox partner. However, our studies with hepatic cytochrome P450-reductase… CONTINUE READING
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