Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2078961 | Chinese Journal of Biotechnology | 2007 | 4 Pages |
Abstract
Bacillus pumilus xylanase was cloned and sequenced. Based on the tertiary structure that originated from homology modeling, the potential active pocket was searched and ligand-protein docking was performed using relative softwares. The information extracted from the molecular docking was analyzed; several amino acid residues that may play a vital role in the xylanase catalytic reaction were obtained to instruct the further modification of xylanase directed-evolution.
Keywords
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Biotechnology
Authors
LIN Jin-Xia, ZHANG Liao-Yuan, ZHANG Guang-Ya, FANG Bai-Shan,