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首页> 外文期刊>FEBS Letters >The identification of the acid–base catalyst of α‐arabinofuranosidase from Geobacillus stearothermophilus T‐6, a family 51 glycoside hydrolase
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The identification of the acid–base catalyst of α‐arabinofuranosidase from Geobacillus stearothermophilus T‐6, a family 51 glycoside hydrolase

机译:从嗜热脂肪芽孢杆菌T-6(一种51糖苷水解酶)中鉴定α-阿拉伯呋喃糖苷酶的酸碱催化剂

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摘要

>The α- class="smallCaps">L-arabinofuranosidase from Geobacillus stearothermophilus T-6 (AbfA T-6) belongs to the retaining family 51 glycoside hydrolases. The conserved Glu175 was proposed to be the acid–base catalytic residue. AbfA T-6 exhibits residual activity towards aryl β- class="smallCaps">D-xylopyranosides. This phenomenon was used to examine the catalytic properties of the putative acid–base mutant E175A. Data from kinetic experiments, pH profiles, azide rescue, and the identification of the xylopyranosyl azide product provide firm support to the assignment of Glu175 as the acid–base catalyst of AbfA T-6.
机译:>来自嗜热脂肪芽孢杆菌T-6(AbfA T-6)的α- class =“ smallCaps”> L -阿拉伯呋喃糖苷酶属于保留家族51糖苷水解酶。保守的Glu175被认为是酸碱催化残基。 AbfA T-6对芳基β- class =“ smallCaps”> D -吡喃吡喃糖苷具有残留活性。该现象用于检查推定的酸碱突变体E175A的催化性能。动力学实验,pH曲线,叠氮化物拯救以及木吡喃葡萄糖基叠氮化物产物的鉴定数据为将Glu175指派为AbfA T-6的酸碱催化剂提供了有力的支持。

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