Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity.

@article{Watanabe1993IdentificationOG,
  title={Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity.},
  author={T. Watanabe and K. Kobori and K. Miyashita and T. Fujii and H. Sakai and M. Uchida and H. Tanaka},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 25},
  pages={
          18567-72
        }
}
Prokaryotic chitinases, class III plant chitinases, yeast chitinases, and endo-beta-N-acetylglucosaminidases share weak amino acid sequence similarities at the certain region of each enzyme. These regions have been assumed to be important for catalytic activities of the enzymes. To verify this assumption, three amino acid residues (Ser-160, Asp-200, Glu-204) in chitinase A1 of Bacillus circulans WL-12 were chosen, based on the amino acid sequence alignment of the regions sharing sequence… Expand
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