Structural highlights
Function
XYNA_HALH5
Publication Abstract from PubMed
The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.
Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.,Suzuki M, Takita T, Kuwata K, Nakatani K, Li T, Katano Y, Kojima K, Mizutani K, Mikami B, Yatsunami R, Nakamura S, Yasukawa K Biosci Biotechnol Biochem. 2021 Feb 18;85(2):386-390. doi: 10.1093/bbb/zbaa003. PMID:33604642[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suzuki M, Takita T, Kuwata K, Nakatani K, Li T, Katano Y, Kojima K, Mizutani K, Mikami B, Yatsunami R, Nakamura S, Yasukawa K. Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E. Biosci Biotechnol Biochem. 2021 Feb 18;85(2):386-390. doi: 10.1093/bbb/zbaa003. PMID:33604642 doi:http://dx.doi.org/10.1093/bbb/zbaa003
