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 language | English |
|---|---|
| Pages (from-to) | 74-78 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 494 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 2001 Apr 6 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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}
Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1. / Watanabe, Takeshi; Ishibashi, Asuka; Ariga, Yumiko; Hashimoto, Masayuki; Nikaidou, Naoki; Sugiyama, Junji; Matsumoto, Takuo; Nonaka, Takamasa.
In: FEBS Letters, Vol. 494, No. 1-2, 06.04.2001, p. 74-78.Research output: Contribution to journal › Article
TY - JOUR
T1 - Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline chitin hydrolysis by Bacillus circulans chitinase A1
AU - Watanabe, Takeshi
AU - Ishibashi, Asuka
AU - Ariga, Yumiko
AU - Hashimoto, Masayuki
AU - Nikaidou, Naoki
AU - Sugiyama, Junji
AU - Matsumoto, Takuo
AU - Nonaka, Takamasa
PY - 2001/4/6
Y1 - 2001/4/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0035815378&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035815378&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(01)02317-1
DO - 10.1016/S0014-5793(01)02317-1
M3 - Article
C2 - 11297738
AN - SCOPUS:0035815378
VL - 494
SP - 74
EP - 78
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -