Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of deacetoxycephalosporin C synthase.

@article{Oster2004ConformationalFO,
  title={Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of deacetoxycephalosporin C synthase.},
  author={Linda M Oster and Anke C. Terwisscha van Scheltinga and Karin Valeg{\aa}rd and Alasdair MacKenzie Hose and Alain Dubus and J{\'a}nos Hajdu and Inger Andersson},
  journal={Journal of molecular biology},
  year={2004},
  volume={343 1},
  pages={157-71}
}
Deacetoxycephalosporin C synthase (DAOCS) from Streptomyces clavuligerus catalyses the oxidative ring expansion of the penicillin nucleus into the nucleus of cephalosporins. The reaction requires dioxygen and 2-oxoglutarate as co-substrates to create a reactive iron-oxygen intermediate from a ferrous iron in the active site. The active enzyme is monomeric in solution. The structure of DAOCS was determined earlier from merohedrally twinned crystals where the last four C-terminal residues (308… CONTINUE READING