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

研究成果: Article同行評審

45 引文 斯高帕斯(Scopus)

摘要

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.

原文English
頁(從 - 到)74-78
頁數5
期刊FEBS Letters
494
發行號1-2
DOIs
出版狀態Published - 2001 4月 6

All Science Journal Classification (ASJC) codes

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 分子生物學
  • 遺傳學
  • 細胞生物學

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