Stereoselectivity and Conformational Stability of Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110: The Effect of pH and Temperature.
| Autoři | |
|---|---|
| Rok publikování | 2011 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | FEBS Journal |
| Fakulta / Pracoviště MU | |
| Citace | |
| Doi | http://dx.doi.org/10.1111/j.1742-4658.2011.08203.x |
| Obor | Biochemie |
| Klíčová slova | DbJA; Enantioselectivity;Haloalkane Dehalogenase |
| Popis | The effect of pH and temperature on structure, stability, activity and enantioselectivity of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110 was investigated in this study. Conformational changes have been assessed by circular dichroism spectroscopy, functional changes by kinetic analysis, while quaternary structure was studied by gel filtration chromatography. Our study shows that the DbjA enzyme is highly tolerant to pH changes. Its secondary and tertiary structure was not affected by pH in the range of 5.3-10.3 and 6.2-10.1, respectively. Oligomerization of DbjA was strongly pH-dependent: monomer, dimer, tetramer and a high molecular weight cluster of the enzyme was distinguished in solution at different pH conditions. Moreover, different oligomeric states of DbjA possessed different thermal stability. |
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