Title |
Stepwise enhancement of catalytic performance of haloalkane dehalogenase LinB towards β-hexachlorocyclohexane
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Published in |
AMB Express, September 2014
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DOI | 10.1186/s13568-014-0072-5 |
Pubmed ID | |
Authors |
Ryota Moriuchi, Hiroki Tanaka, Yuki Nikawadori, Mayuko Ishitsuka, Michihiro Ito, Yoshiyuki Ohtsubo, Masataka Tsuda, Jiri Damborsky, Zbynek Prokop, Yuji Nagata |
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. |
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