Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima
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...
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Format: | Article |
Language: | English |
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Elsevier
2015-12-01
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Series: | Data in Brief |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340915002127 |
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author | Mohammad S. Eram Benozir Sarafuddin Frank Gong Kesen Ma |
author_facet | Mohammad S. Eram Benozir Sarafuddin Frank Gong Kesen Ma |
author_sort | Mohammad S. Eram |
collection | DOAJ |
description | 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. |
first_indexed | 2024-12-10T05:52:02Z |
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id | doaj.art-3c7a0f63181a4359863bd3df2757b81c |
institution | Directory Open Access Journal |
issn | 2352-3409 |
language | English |
last_indexed | 2024-12-10T05:52:02Z |
publishDate | 2015-12-01 |
publisher | Elsevier |
record_format | Article |
series | Data in Brief |
spelling | doaj.art-3c7a0f63181a4359863bd3df2757b81c2022-12-22T02:00:01ZengElsevierData in Brief2352-34092015-12-015C48949710.1016/j.dib.2015.09.018Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritimaMohammad S. EramBenozir SarafuddinFrank GongKesen MaThe 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.http://www.sciencedirect.com/science/article/pii/S2352340915002127Acetohydroxyacid synthaseHyperthermophilesThermotogaHeat-treatment |
spellingShingle | Mohammad S. Eram Benozir Sarafuddin Frank Gong Kesen Ma Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima Data in Brief Acetohydroxyacid synthase Hyperthermophiles Thermotoga Heat-treatment |
title | Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima |
title_full | Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima |
title_fullStr | Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima |
title_full_unstemmed | Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima |
title_short | Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima |
title_sort | optimization of expression and properties of the recombinant acetohydroxyacid synthase of thermotoga maritima |
topic | Acetohydroxyacid synthase Hyperthermophiles Thermotoga Heat-treatment |
url | http://www.sciencedirect.com/science/article/pii/S2352340915002127 |
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