Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1

Takeshi Watanabe, Asuka Ishibashi, Yumiko Ariga, Masayuki Hashimoto, Naoki Nikaidou, Junji Sugiyama, Takuo Matsumoto, Takamasa Nonaka

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45 Citations (Scopus)

Abstract

From the 3D-structural analysis of the catalytic domain of chitinase A1, two exposed tryptophan residues (W122 and W134) are proposed to play an important role in guiding a chitin chain into the catalytic cleft during the crystalline chitin hydrolysis. Mutation of either W122 or W134 to alanine significantly reduced the hydrolyzing activity against highly crystalline β-chitin microfibrils. Double mutation almost completely abolished the hydrolyzing activity. On the other hand, the hydrolyzing activity against either soluble or amorphous substrate was not reduced. These mutations slightly impaired the binding activity of this enzyme. These results clearly demonstrated that the two exposed aromatic residues play a critical role in hydrolyzing the chitin chain in crystalline chitin.

Original languageEnglish
Pages (from-to)74-78
Number of pages5
JournalFEBS Letters
Volume494
Issue number1-2
DOIs
Publication statusPublished - 2001 Apr 6

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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