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首页> 外文期刊>Journal of bacteriology >Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli.
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Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli.

机译:大肠杆菌的温度敏感泛酸激酶(coaA)突变体的分离和表征。

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Escherichia coli mutants conditionally defective in the conversion of pantothenate to coenzyme A were isolated and characterized. The gene was designated coaA and localized between argEH and rpoB near min 90 of the chromosome. The coaA15(Ts) mutation caused a temperature-sensitive growth phenotype and temperature-dependent inactivation of pantothenate kinase activity assayed both in vivo and in vitro. At 30 degrees C, coaA15(Ts) extracts contained less than 20% of the wild-type pantothenate kinase activity; the kinase had near normal kinetic constants for the substrates ATP and pantothenate and was inhibited by coenzyme A to the same degree as the wild-type enzyme. These data define the coaA gene as the structural gene for pantothenate kinase.
机译:分离并鉴定了在泛酸向辅酶A转化中有条件缺陷的大肠杆菌突变体。该基因被命名为coaA,位于染色体90分钟附近的argEH和rpoB之间。 coaA15(Ts)突变引起体内和体外测定的泛酸激酶活性的温度敏感型生长表型和温度依赖性失活。在30摄氏度时,coaA15(Ts)提取物的野生型泛酸激酶活性不到20%;该激酶对底物ATP和泛酸具有接近正常的动力学常数,并且被辅酶A抑制的程度与野生型酶相同。这些数据将coaA基因定义为泛酸激酶的结构基因。

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