Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis.

@article{Bohc2002HalidestabilizingRO,
  title={Halide-stabilizing residues of haloalkane dehalogenases studied by quantum mechanic calculations and site-directed mutagenesis.},
  author={Michal Boh{\'a}c and Yuji Nagata and Zbynek Prokop and Martin Prokop and Marta Monincov{\'a} and Masataka Tsuda and Jaroslav Ko{\vc}a and Jiř{\'i} Damborsk{\'y}},
  journal={Biochemistry},
  year={2002},
  volume={41 48},
  pages={14272-80}
}
Haloalkane dehalogenases catalyze cleavage of the carbon-halogen bond in halogenated aliphatic compounds, resulting in the formation of an alcohol, a halide, and a proton as the reaction products. Three structural features of haloalkane dehalogenases are essential for their catalytic performance: (i) a catalytic triad, (ii) an oxyanion hole, and (iii) the halide-stabilizing residues. Halide-stabilizing residues are not structurally conserved among different haloalkane dehalogenases. The level… CONTINUE READING