Kinetic and physical characterisation of recombinant wild-type and mutant human protoporphyrinogen oxidases.

@article{Maneli2003KineticAP,
  title={Kinetic and physical characterisation of recombinant wild-type and mutant human protoporphyrinogen oxidases.},
  author={Mbulelo H Maneli and Anne V. Corrigall and Horst H. Klump and Lester M. Davids and Ralph E. Kirsch and Peter Mei\ssner},
  journal={Biochimica et biophysica acta},
  year={2003},
  volume={1650 1-2},
  pages={10-21}
}
The effects of various protoporphyrinogen oxidase (PPOX) mutations responsible for variegate porphyria (VP), the roles of the arginine-59 residue and the glycines in the conserved flavin binding site, in catalysis and/or cofactor binding, were examined. Wild-type recombinant human PPOX and a selection of mutants were generated, expressed, purified and partially characterised. All mutants had reduced PPOX activity to varying degrees. However, the activity data did not correlate with the ability… CONTINUE READING

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Quantitative structural insight into human variegate porphyria disease.

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