CYP2E1 substrate inhibition. Mechanistic interpretation through an effector site for monocyclic compounds.

@article{Collom2008CYP2E1SI,
  title={CYP2E1 substrate inhibition. Mechanistic interpretation through an effector site for monocyclic compounds.},
  author={Samuel L. Collom and Ryan M. Laddusaw and Amber M Burch and Petr Kuzmi{\vc} and Martin D Perry and Grover P Miller},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 6},
  pages={
          3487-96
        }
}
In this study we offer a mechanistic interpretation of the previously known but unexplained substrate inhibition observed for CYP2E1. At low substrate concentrations, p-nitrophenol (pNP) was rapidly turned over (47 min(-1)) with relatively low K(m) (24 microM); nevertheless, at concentrations of >100 microM, the rate of pNP oxidation gradually decreased as a second molecule bound to CYP2E1 through an effector site (K(ss) = 260 microm), which inhibited activity at the catalytic site. 4… CONTINUE READING

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