Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.

@article{Binda2000CrosstalkAA,
  title={Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase.},
  author={Claudia Binda and Roberto T Bossi and Soichi Wakatsuki and Steffi Arzt and Alessandro Coda and Bruno Curti and Maria Antonietta Vanoni and Andrea Mattevi},
  journal={Structure},
  year={2000},
  volume={8 12},
  pages={1299-308}
}
INTRODUCTION The complex iron-sulfur flavoprotein glutamate synthase catalyses the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine, a reaction in the plant and bacterial pathway for ammonia assimilation. The enzyme functions through three distinct active centers carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor. RESULTS The 3.0 A crystal structure of the dimeric 324 kDa core protein of a… CONTINUE READING
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