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.
Author: Ryota MoriuchiHiroki TanakaYuki NikawadoriMayuko IshitsukaMichihiro ItoYoshiyuki OhtsuboMasataka TsudaJiri DamborskyZbynek ProkopYuji Nagata
Credits/Source: AMB Express 2014, 4:72
Published on: 2014-09-21
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