Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.

@article{Litzinger2010StructuralAK,
  title={Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism.},
  author={Silke Litzinger and Stefanie Fischer and Patrick Polzer and Kay Diederichs and Wolfram Welte and Christoph Mayer},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 46},
  pages={
          35675-84
        }
}
Three-dimensional structures of NagZ of Bacillus subtilis, the first structures of a two-domain β-N-acetylglucosaminidase of family 3 of glycosidases, were determined with and without the transition state mimicking inhibitor PUGNAc bound to the active site, at 1.84- and 1.40-Å resolution, respectively. The structures together with kinetic analyses of mutants revealed an Asp-His dyad involved in catalysis: His(234) of BsNagZ acts as general acid/base catalyst and is hydrogen bonded by Asp(232… CONTINUE READING

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