Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170.

@article{Uchiyama2001RolesOT,
  title={Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170.},
  author={Taku Uchiyama and Fuminori Katouno and Naoki Nikaidou and Takamasa Nonaka and Junji Sugiyama and Takashi Watanabe},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 44},
  pages={
          41343-9
        }
}
Four exposed aromatic residues, two in the N-terminal domain (Trp-69 and Trp-33) and two in the catalytic domain (Trp-245 and Phe-232) of Serratia marcescens chitinase A, are linearly aligned with the deep catalytic cleft. To investigate the importance of these residues in the binding activity and hydrolyzing activity against insoluble chitin, site-directed mutagenesis to alanine was carried out. The substitution of Trp-69, Trp-33, or Trp-245 significantly reduced the binding activity to both… CONTINUE READING
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