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Literature summary extracted from

  • Nakani, S.; Viriyakul, T.; Mitchell, R.; Vitello, L.B.; Erman, J.E.
    Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase (2006), Biochemistry, 45, 9887-9893.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.5 E290C formation of a covalent complex with cytochrome c mutant K79C, kinetic studies. Residual activity of complex is due to unreacted enzyme that copurifies with the complex. In the complex, the Pelletier-Kraut site is blocked which results in zero catalytic activity Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.5 0.002
-
 ferrocytochrome c recombinant wild-type, pH 7.5, 25°C, 100 mM phosphate buffer Saccharomyces cerevisiae
1.11.1.5 0.011
-
 ferrocytochrome c covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex Saccharomyces cerevisiae
1.11.1.5 0.047
-
 ferrocytochrome c recombinant wild-type, pH 7.5, 25°C, 10 mM phosphate buffer Saccharomyces cerevisiae
1.11.1.5 0.13
-
 ferrocytochrome c covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.5 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.11.1.5 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O only ferrocytochrome c bound at the Pelletier-Kraut site of enzyme is oxidized during turnover Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.5 ferrocytochrome c + H2O2
-
 Saccharomyces cerevisiae ferricytochrome c + 2 H2O
-
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