Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway.

@article{Kanno2005StructurebasedIV,
  title={Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway.},
  author={Takuya Kanno and Akira Komatsu and Koji Kasai and Joseph Gogo Dubouzet and Minako Sakurai and Yasuko Ikejiri-Kanno and Kyo Wakasa and Yuzuru Tozawa},
  journal={Plant physiology},
  year={2005},
  volume={138 4},
  pages={2260-8}
}
Rice (Oryza sativa) anthranilate synthase alpha-subunit, OASA2, was modified by in vitro mutagenesis based on structural information from bacterial homologs. Twenty-four amino acid residues, predicted as putative tryptophan binding sites or their proximal regions in the OASA2 sequence, were selected and 36 mutant OASA2 genes were constructed by PCR-based site-directed mutagenesis. Corresponding mutant proteins were synthesized in a combination of two in vitro systems, transcription with a… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

Cell-Free Protein Production

Endo Kazuyuki Takai Takuya Ueda
Methods in Molecular Biology • 2010
View 9 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…