Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.

@article{Li1998CrystalSO,
  title={Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism.},
  author={Yong Feng Li and Yutaka Hata and Tomomi Fujii and T. Hisano and Masateru Nishihara and Tatsuo Kurihara and Nobuyoshi Esaki},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 24},
  pages={15035-44}
}
Crystal structures of L-2-haloacid dehalogenase from Pseudomonas sp. YL complexed with monochloroacetate, L-2-chlorobutyrate, L-2-chloro-3-methylbutyrate, or L-2-chloro-4-methylvalerate were determined at 1.83-, 2.0-, 2.2-, and 2.2-A resolutions, respectively, using the complex crystals prepared with the S175A mutant, which are isomorphous with those of the wild-type enzyme. These structures exhibit unique structural features that correspond to those of the reaction intermediates. In each case… CONTINUE READING