Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards Beta-Hexachlorocyclohexane.
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Article in Periodical |
| Magazine / Source | Applied Microbiology and Biotechnology Express |
| MU Faculty or unit | |
| Citation | |
| Web | Full Text |
| Doi | http://dx.doi.org/10.1186/s13568-014-0072-5 |
| Field | Biochemistry |
| Keywords | beta -Hexachlorocyclohexane; Xenobiotics; Biodegradation; Haloalkane dehalogenase; Protein evolution |
| Description | Two haloalkane dehalogenases, LinBUT and LinBMI, each with 296 amino acid (aa) residues, exhibit only seven amino acid residue differences between them, but LinBMI‘s catalytic performance towards beta-hexachlorocyclohexane (beta-HCH) is considerably higher than LinBUT‘s. To elucidate the molecular basis governing this difference, intermediate mutants between LinBUT and LinBMI were constructed and kinetically characterized. The activities of LinBUT-based mutants gradually increased by cumulative mutations into LinBUT, and the effects of the individual amino acid substitutions depended on combination with other mutations. These results indicated that LinBUT‘s b-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations. |
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