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首页> 外文期刊>Microbiology >The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity
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The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity

机译:芽孢杆菌的乙酰Xylan酯酶属于具有宽底物特异性的酯酶家族

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摘要

The Bacillus pumilus gene encoding acetyl xylan esterase (axe) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) purified from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar size and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.
机译:鉴定编码乙酰木聚糖酯酶(AX)的芽孢杆菌基因。表达轴基因,纯化大肠杆菌中产生的重组酶被纯化并表征。重组酶向纯化的B.Pumilus纯化的乙酰Xylan酯酶(AX)与乙酰Xylan酯酶(AX)显示出类似的性质。斧头初级结构与B.枯草芽孢杆菌的头孢菌素C脱乙酰酶相同76%,枯草芽孢杆菌和40%至来自Thermootogacterium和Thermotoga Maritima最近识别的轴。这四种蛋白质具有相似的大小,并且代表具有宽底物特异性的新酯酶。将重组轴证明在几种乙酰化基材上具有活性,包括在头孢菌素C上。

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