Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel.

@article{Chaloupkova2003ModificationOA,
  title={Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel.},
  author={Radka Chaloupkova and J. S{\'y}korov{\'a} and Zbynek Prokop and Andrea Jesensk{\'a} and Marta Monincov{\'a} and Martina Pavlov{\'a} and Masataka Tsuda and Yuji Nagata and Jiř{\'i} Damborsk{\'y}},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 52},
  pages={52622-8}
}
Structural comparison of three different haloalkane dehalogenases suggested that substrate specificity of these bacterial enzymes could be significantly influenced by the size and shape of their entrance tunnels. The surface residue leucine 177 positioned at the tunnel opening of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26 was selected for modification based on structural and phylogenetic analysis; the residue partially blocks the entrance tunnel, and it is the most variable… CONTINUE READING

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