Differential roles of Glu318 and Thr319 in cytochrome P450 1A2 catalysis supported by NADPH-cytochrome P450 reductase and tert-butyl hydroperoxide.

@article{Hiroya1994DifferentialRO,
  title={Differential roles of Glu318 and Thr319 in cytochrome P450 1A2 catalysis supported by NADPH-cytochrome P450 reductase and tert-butyl hydroperoxide.},
  author={Kou Hiroya and Yasuoki Murakami and Toru Shimizu and Masahiro Hatano and Paul R. Ortiz de Montellano},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={310 2},
  pages={397-401}
}
The kinetic values for 7-ethoxycoumarin (7-EC) hydroxylation have been obtained in both the NADPH-cytochrome P450 reductase- and tert-butyl hydroperoxide (TBHP)-supported systems for several Glu318 and Thr319 mutants of cytochrome P450 1A2. The results with the reductase-supported system suggest that Glu318 is important for both substrate binding and catalysis, whereas Thr319 is critical for neither, although the size of the residue at position 319 influences catalytic activity. In contrast… CONTINUE READING