Nakamura S, Nakai R, Namba K, Kubo T, Wakabayashi K, Aono R, Horikoshi K
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Nucleic Acids Symp Ser. 1995(34):99-100.
Xylanase J from alkaliphilic Bacillus sp. strain 41M-1 contains a family G catalytic domain at the N-terminus, followed by a linker sequence and a functionally-unknown C-terminal domain. The mutational analysis of xylanase J indicated that Glu-93, Glu-183, Trp-18, Trp-86, Tyr-84 and Tyr-95 play an important role in the catalytic activity. A deletion derivative of xylanase J lacking the C-terminal domain retained its activity, suggesting that the C-terminal domain does not directly involved in catalysis.
来自嗜碱芽孢杆菌菌株41M-1的木聚糖酶J在N端含有一个G家族催化结构域，随后是一个连接序列和一个功能未知的C端结构域。木聚糖酶J的突变分析表明，Glu-93、Glu-183、Trp-18、Trp-86、Tyr-84和Tyr-95在催化活性中起重要作用。缺少C端结构域的木聚糖酶J缺失衍生物保留了其活性，这表明C端结构域不直接参与催化作用。
