Abstract
Two haloalkane dehalogenases, LinBUT and LinBMI, each with 296 amino acid residues, exhibit only seven amino acid residue differences between them, but LinBMI’s catalytic performance towards β-hexachlorocyclohexane (β-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 β-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations.
Original language | English |
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Article number | 72 |
Pages (from-to) | 1-10 |
Number of pages | 10 |
Journal | AMB Express |
Volume | 4 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2014 Dec 1 |
Keywords
- Biodegradation
- Haloalkane dehalogenase
- Protein evolution
- Xenobiotics
- β-Hexachlorocyclohexane
ASJC Scopus subject areas
- Biophysics
- Applied Microbiology and Biotechnology