Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.

@article{Axe2015SeveringOA,
  title={Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.},
  author={Jennifer M Axe and Kathleen F. O'Rourke and Nicole E Kerstetter and Eric M Yezdimer and Yan Mei Chan and A. Chasin and David D. Boehr},
  journal={Protein science : a publication of the Protein Society},
  year={2015},
  volume={24 4},
  pages={484-94}
}
Conformational changes in the β2α2 and β6α6 loops in the alpha subunit of tryptophan synthase (αTS) are important for enzyme catalysis and coordinating substrate channeling with the beta subunit (βTS). It was previously shown that disrupting the hydrogen bond interactions between these loops through the T183V substitution on the β6α6 loop decreases… CONTINUE READING