Mechanism-based in vivo inactivation of lauric acid hydroxylases.

@article{Cajacob1986MechanismbasedIV,
  title={Mechanism-based in vivo inactivation of lauric acid hydroxylases.},
  author={Claire A Cajacob and Paul R. Ortiz de Montellano},
  journal={Biochemistry},
  year={1986},
  volume={25 16},
  pages={4705-11}
}
The hepatic cytochrome P-450 isozymes that catalyze omega- and (omega - 1)-hydroxylation of lauric acid are specifically inactivated in vitro but not in vivo by 10-undecynoic acid. The lack of in vivo activity may result from rapid degradation of the inhibitor by beta-oxidation. Strategies for the construction of fatty acid analogues that retain the ability to inactivate fatty acid hydroxylases but are resistant to metabolic degradation have therefore been sought. Fatty acid analogues in which… CONTINUE READING