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Literature summary for 1.11.1.5 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
Search for more literature for 1.11.1.5

Inhibitors

Inhibitors Comment Organism Structure
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
H2O2 2 mM, noticeably retards the growth of the enzyme gene disrupted mutants Saccharomyces cerevisiae

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + H2O2
-
 Saccharomyces cerevisiae ferricytochrome c + H2O
-
 ?