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Literature summary extracted from

  • Kwon, M.; Chong, S.; Han, S.; Kim, K.
    Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae (2003), Biochim. Biophys. Acta, 1623, 1-5.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.5 3-Amino-1,2,4-triazole 2 mM, in the presence of 2 mM H2O2, noticeably retards the growth of the enzyme gene disrupted mutants Saccharomyces cerevisiae
1.11.1.5 H2O2 2 mM, noticeably retards the growth of the enzyme gene disrupted mutants Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.5 mitochondrial intermembrane space
-
Saccharomyces cerevisiae 5758
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.5 ferrocytochrome c + H2O2 Saccharomyces cerevisiae
-
ferricytochrome c + H2O
-
?

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 the enzyme uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c. The enzyme is not essential for both cell viability and respiration. Its biological function is to reduce H2O2 generated during aerobic respiratory process. The enzyme may also act as a peroxynitrite scavenger Saccharomyces cerevisiae

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 + H2O
-
?