Spectroscopic studies of isopenicillin N synthase. A mononuclear nonheme Fe2+ oxidase with metal coordination sites for small molecules and substrate.

@article{Chen1989SpectroscopicSO,
  title={Spectroscopic studies of isopenicillin N synthase. A mononuclear nonheme Fe2+ oxidase with metal coordination sites for small molecules and substrate.},
  author={Victor J. Chen and Allen M. Orville and Mark R Harpel and Charles A. Frolik and Kristene K. Surerus and Eckard M{\"u}nck and John D Lipscomb},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 36},
  pages={21677-81}
}
The nonheme iron oxidase isopenicillin N synthase catalyzes the formation of two new internal bonds in the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to form the beta-lactam and thiazolidine rings of isopenicillin N. Concomitantly, O2 is reduced to 2 H2O. The recombinant enzyme from Cephalosporium acremonium (Mr = 38,400), expressed… CONTINUE READING