Wild-type and mutant forms of recombinant horseradish peroxidase C expressed in Escherichia coli. Substrate specificity and stability under irradiation.

@article{Mareeva1996WildtypeAM,
  title={Wild-type and mutant forms of recombinant horseradish peroxidase C expressed in Escherichia coli. Substrate specificity and stability under irradiation.},
  author={E A Mareeva and Marina A. Orlova and Victoria Doseeva and D B Loginov and Andrey G Galkin and I G Gazarian and Vladimir I. Tishkov},
  journal={Applied biochemistry and biotechnology},
  year={1996},
  volume={61 1-2},
  pages={13-23}
}
Two horseradish peroxidase C (HRPC) mutants with substitutions in the active center, i.e., Phe41-->His and Phe143-->Glu, were compared to the wild-type recombinant enzyme expressed in Escherichia coli in terms of the enzymatic activity and stability under irradiation. Both mutations caused a significant decrease in activity, but it was still possible to follow the effect of mutations on the key steps of the reaction mechanism. Phe41 can be considered a nonpolar barrier separating histidine… CONTINUE READING

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