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Literature summary for 1.11.1.5 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
Search for more literature for 1.11.1.5

Protein Variants

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

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
-
 bakers´ yeast
-

Substrates and Products (Substrate)

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

pH Range

pH Minimum pH Maximum Comment Organism
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