Structure and Function of a Multidomain Alkaline Xylanase from Alkaliphilic Bacillus Sp. Strain 41M-1
Structure and Function of a Multidomain Alkaline Xylanase from Alkaliphilic Bacillus Sp. Strain 41M-1
复制标题
嗜碱芽孢杆菌多域碱性木聚糖酶的结构和功能。
DOI：
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Satoshi Nakamura
中科院分区：
文献类型：
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作者：
Satoshi Nakamura
Xylanase is an enzyme that catalyzes the hydrolysis of xylan, a β-1,4-linked xylose polymer. Alkaliphilic Bacillus sp. strain 41M-1 secretes a xylanase (xylanase J) that has an alkaline pH optimum. Xylanase J is a multidomain enzyme and consists of two functional domains: a family 11/G catalytic domain and a non-catalytic xylan-binding domain. The xylan-binding domain bound to xylan and enhanced catalytic activity of the adjacent catalytic domain. Mutational analyses revealed some amino acid residues that contribute to catalytic activity, alkaliphily and xylan-binding activity of xylanase J.
影响因子：
3.5
作者：
PARMLEY, SF;SMITH, GP
通讯作者：
SMITH, GP