| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 174900 | Data in Brief | 2015 | 9 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Mohammad S. Eram, Benozir Sarafuddin, Frank Gong, Kesen Ma,