马里蒂玛热带鱼
大肠杆菌
重组DNA
酶
生物化学
基因
超嗜热菌
ATP合酶
生物
计算生物学
遗传学
古细菌
作者
Mohammad S. Eram,Benozir Sarafuddin,Frank Gong,Kesen Ma
出处
期刊:Data in Brief
[Elsevier BV]
日期:2015-10-10
卷期号:5: 489-497
被引量:2
标识
DOI:10.1016/j.dib.2015.09.018
摘要
The data provide additional support of the characterization of the biophysical and biochemical properties of the enzyme acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima (Eram et al., 2015) [1]. The genes encoding the enzyme subunits have been cloned and expressed in the mesophilic host Escherichia coli. Detailed data include information about the optimization of the expression conditions, biophysical properties of the enzyme and reconstitution of the holoenzyme from individually expressed and purified subunits.
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