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Literature summary extracted from

  • Bidwai, A.; Witt, M.; Foshay, M.; Vitello, L.B.; Satterlee, J.D.; Erman, J.E.
    Cyanide binding to cytochrome c peroxidase (H52L) (2003), Biochemistry, 42, 10764-10771.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.5 H52L with slower cyanide dissociation rate constant for the heme group with respect to the wild-type enzyme Saccharomyces cerevisiae

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
-
bakers´ yeast
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.5 ferrocytochrome c + CN- dominant binding pathway for H52L mutant, biphasic reaction Saccharomyces cerevisiae ?
-
?
1.11.1.5 ferrocytochrome c + H2O2
-
Saccharomyces cerevisiae ferricytochrome c + H2O
-
?
1.11.1.5 ferrocytochrome c + HCN dominant binding pathway for wild-type enzyme Saccharomyces cerevisiae ?
-
?

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.11.1.5 4 8.6 the association rate constant for the binding of cyanide to H52L mutant varies almost 4 orders of magnitude in this pH range. Above pH 8 cyanide binds more rapidly to H52L mutant than to wild-type enzyme Saccharomyces cerevisiae