| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2021868 | Protein Expression and Purification | 2007 | 9 Pages |
Abstract
The purified SXL-G311D and SXL-G311K mutants show distinct pH profiles. The SXL-G311D mutant is optimally active at pH 6.5, whereas, the SXL-G311K mutant is active at pH 9.5. In addition, these two mutants show an important decrease in the specific activities that generates a decrease in the catalytic efficiency (kcat/Kmapp.). We can essentially notice that the SXL-G311K mutant displays a 33- or 44-fold decrease in kcat/Kmapp. values compared to the SXL-WT, when using TC4 or TC8 as substrate, respectively.
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Biochemistry
Authors
Habib Mosbah, Adel Sayari, Habib Horchani, Youssef Gargouri,