MANNOSE FORAGING BY BACTEROIDES THETAIOTAOMICRON Structure and specificity of the β -mannosidase, Man2A
MANNOSE FORAGING BY BACTEROIDES THETAIOTAOMICRON Structure and specificity of the β -mannosidase, Man2A
复制标题
拟杆菌采集甘露糖 β-甘露糖苷酶 Man2A 的结构和特异性
DOI：
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发表时间：
2007
期刊：
影响因子：
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通讯作者：
H. Gilbert
中科院分区：
文献类型：
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作者：
L. Tailford;V. A. Money;N. Smith;Claire Dumon;G. Davies;H. Gilbert
specific for manno configured substrates. Mutagenesis studies, informed by the crystal structure, identified a WDW motif in the N-terminal domain that makes a significant contribution to catalytic activity. The observation that this motif is invariant in GH2 mannosidases points to a generic role for these residues in this enzyme class. The identification of GH-A clan and GH2 specific residues in the active site of Bt GH2 explains why this enzyme is able to harness substrate binding at the proximal glycone binding site more efficiently than mannan-hydrolysing glycoside hydrolases in related enzyme families.
