Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast. Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway.

@article{Urban1994CharacterizationOR,
  title={Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast. Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway.},
  author={Philippe Urban and Daniele Werck-reichhart and H G Teutsch and Francis Durst and Sophie R{\'e}gnier and Micha{\"e}l Kazmaier and Denis Pompon},
  journal={European journal of biochemistry},
  year={1994},
  volume={222 3},
  pages={843-50}
}
Helianthus tuberosus cinnamate 4-hydroxylase (CYP73 or CA4H), a member of the P450 superfamily which catalyses the first oxidative step of the phenylpropanoid pathway in higher plants by transforming cinnamate into p-coumarate, was expressed in the yeast Saccharomyces cerevisiae. The PCR-amplified CA4H open reading frame was inserted into pYeDP60 under the transcriptional control of a galactose-inducible artificial promoter. Engineered S. cerevisiae strains producing human P450 reductase or… CONTINUE READING