Site-directed mutagenesis and oxygen isotope incorporation studies of the nucleophilic aspartate of haloalkane dehalogenase.

@article{Pries1994SitedirectedMA,
  title={Site-directed mutagenesis and oxygen isotope incorporation studies of the nucleophilic aspartate of haloalkane dehalogenase.},
  author={Frens Pries and Jaap Kingma and M Pentenga and Gertie van Pouderoyen and C. Margot Jeronimus-Stratingh and Andries P. Bruins and Dick B. Janssen},
  journal={Biochemistry},
  year={1994},
  volume={33 5},
  pages={
          1242-7
        }
}
Haloalkane dehalogenase catalyzes the hydrolytic cleavage of carbon-halogen bonds in a broad range of halogenated aliphatic compounds. The X-ray structure suggests that Asp124, which is located close to an internal cavity, carries out a nucleophilic attack on the C alpha of the substrate, releasing the halogen. To study the mechanism of hydrolysis, this aspartate residue was mutated to alanine, glycine, or glutamate. The mutant enzymes showed no activity toward 1,2-dichloroethane and 1,2… CONTINUE READING

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