Recombinant plasmepsin 1 from the human malaria parasite plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis.

@article{Liu2009RecombinantP1,
  title={Recombinant plasmepsin 1 from the human malaria parasite plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis.},
  author={Peng Liu and Melissa R. Marzahn and Arthur H. Robbins and Hugo Guti{\'e}rrez-de-Ter{\'a}n and David Rodriguez and Scott H. McClung and Stanley M Stevens and C. A. Yowell and J. B. Dame and Robert McKenna and Ben Dunn},
  journal={Biochemistry},
  year={2009},
  volume={48 19},
  pages={4086-99}
}
A mutated form of truncated proplasmepsin 1 (proPfPM1) from the human malaria parasite Plasmodium falciparum, proPfPM1 K110pN, was generated and overexpressed in Escherichia coli. The automaturation process was carried out at pH 4.0 and 4.5, and the optimal catalytic pH of the resulting mature PfPM1 was determined to be pH 5.5. This mature PfPM1 showed comparable binding affinity to peptide substrates and inhibitors with the naturally occurring form isolated from parasites. The S3-S3' subsite… CONTINUE READING

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