Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1.

@article{Hayashi2008StructurebasedDO,
  title={Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1.},
  author={Keiko Hayashi and Hiroshi Sugimoto and Raku Shinkyo and Masato Yamada and Shinnosuke Ikeda and Shin-ichi Ikushiro and Masaki Kamakura and Yoshitsugu Shiro and Toshiyuki Sakaki},
  journal={Biochemistry},
  year={2008},
  volume={47 46},
  pages={11964-72}
}
CYP105A1 from Streptomyces griseolus has the capability of converting vitamin D 3 (VD 3) to its active form, 1alpha,25-dihydroxyvitamin D 3 (1alpha,25(OH) 2D 3) by a two-step hydroxylation reaction. Our previous structural study has suggested that Arg73 and Arg84 are key residues for the activities of CYP105A1. In this study, we prepared a series of single and double mutants by site-directed mutagenesis focusing on these two residues of CYP105A1 to obtain the hyperactive vitamin D 3 hydroxylase… CONTINUE READING

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