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Literature summary for 1.11.1.5 extracted from

  • Tsaprailis, G.; English, A.M.
    Different pathways of radical translocation in yeast cytochrome c peroxidase and its W191F mutant on reaction with H(2)O(2) suggest an antioxidant role (2003), J. Biol. Inorg. Chem., 8, 248-255.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
W191F less efficient at catalytic turnover than the wild-type enzyme Escherichia coli
W51F exhibits extensive dimerization Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Subunits

Subunits Comment Organism
dimer SDS-PAGE, wild type and W191F mutant enzymes Escherichia coli
heterodimer SDS-PAGE, H2O2 oxidation induces heterodimerization between cytochrome c and both wild-type and W191F enzymes, but not with W51F mutant Escherichia coli
More dimerization of wild-type enzyme is observed at H2O2/enzyme ratios of 3 and 10. W191F mutant dimerizes irrespectively of the H2O2/enzyme ratio. W51F mutant exhibits extensive dimerization on H2O2 oxidation and formation of higher molecular weight polymeric species indicating nonspecific crosslinking Escherichia coli
polymer SDS-PAGE, W51F mutant Escherichia coli
trimer SDS-PAGE, W51F mutant Escherichia coli