Multiple substrate binding by cytochrome P450 3A4: estimation of the number of bound substrate molecules.

@article{Kapelyukh2008MultipleSB,
  title={Multiple substrate binding by cytochrome P450 3A4: estimation of the number of bound substrate molecules.},
  author={Yury Kapelyukh and Mark J. I. Paine and Jean-Didier Mar{\'e}chal and Michael J. Sutcliffe and C. R. Wolf and Gordon C. K. Roberts},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2008},
  volume={36 10},
  pages={2136-44}
}
Cytochrome P450 3A4, a major drug-metabolizing enzyme in man, is well known to show non-Michaelis-Menten steady-state kinetics for a number of substrates, indicating that more than one substrate can bind to the enzyme simultaneously, but it has proved difficult to obtain reliable estimates of exactly how many substrate molecules can bind. We have used a simple method involving studies of the effect of large inhibitors on the Hill coefficient to provide improved estimates of substrate… CONTINUE READING

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