Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards β-Hexachlorocyclohexane

Authors

Moriuchi, R., Tanaka, H., Nikawadori, Y., Ishitsuka, M., Ito, M., Ohtsubo, Y., Tsuda, M., Damborsky, J., Prokop, Z., Nagata, Y.

Source

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY EXPRESS 4: 72 (2014)

Abstract

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 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 b-HCH degradation activity can be enhanced in a stepwise manner by the accumulation of point mutations.

Full text

Citation

Moriuchi, R., Tanaka, H., Nikawadori, Y., Ishitsuka, M., Ito, M., Ohtsubo, Y., Tsuda, M., Damborsky, J., Prokop, Z., Nagata, Y., 2014: Stepwise Enhancement of Catalytic Performance of Haloalkane Dehalogenase LinB towards β-Hexachlorocyclohexane. Applied Microbiology and Biotechnology Express 4: 72.

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