Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme.

@article{Laskovics1979PrenyltransferaseKS,
  title={Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme.},
  author={F M Laskovics and J M Krafcik and C. Dale Poulter},
  journal={The Journal of biological chemistry},
  year={1979},
  volume={254 19},
  pages={9458-63}
}
Prenyltransferase catalyzes the sequential, irreversible 1'-4 condensation of isopentenyl-PP with dimethylallyl-PP and geranyl-PP to yield farnesyl-PP. A kinetic study shows substrate inhibition by isopentenyl-PP at concentrations above 0.7 microM when the concentration of geranyl-PP is 1.0 microM or less as a result of binding by the homoallylic substrate to the allylic region of the active site. Inhibition studies were carried out with the products, farnesyl-PP and PPi, and dead-end… CONTINUE READING