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首页> 外文期刊>Pakistan journal of botany >Crystallization of fructose 1,6-bisphosphatase from the hyperthermophilic Archaeon Thermococcus kodakaraensis
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Crystallization of fructose 1,6-bisphosphatase from the hyperthermophilic Archaeon Thermococcus kodakaraensis

机译:从超嗜热古生嗜热球菌中提取果糖1,6-双磷酸酶

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摘要

The enzyme Fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11) is one of the key enzymes of the gluconeogenic pathway. It hydrolyses fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate (Pilkis & Claus, 1991). Here we report the crystallization of FBPase from Thermococcus kodakaraensis. This FBPase consists of 375 amino acids, with a molecular weight of 42kDa, and was prepared using an Escherichia coli expression system. The purified recombinant FBPase was crystallised using the sitting drop vapour-diffusion method at 17°C. Crystals grew tetragonally and measured approximately 0.4 mm in the longest dimension.
机译:果糖-1,6-双磷酸酶(FBPase; EC 3.1.3.11)是糖异生途径的关键酶之一。它将1,6-二磷酸果糖水解为6-磷酸果糖和无机磷酸盐(Pilkis&Claus,1991)。在这里,我们报告了来自嗜热球菌的FBPase的结晶。该FBPase由375个氨基酸组成,分子量为42kDa,并使用大肠杆菌表达系统制备。纯化的重组FBPase在17°C下使用坐滴蒸汽扩散法结晶。晶体呈四边形生长,最长尺寸约为0.4毫米。

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