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Literature summary for 1.11.1.5 extracted from

  • Bidwai, A.K.; Meyen, C.; Kilheeney, H.; Wroblewski, D.; Vitello, L.B.; Erman, J.E.
    Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants (2013), Biochim. Biophys. Acta, 1834, 137-148.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of three apolar distal heme pocket mutants of CcP with altered pH dependencies compared to the wild-type enzyme Saccharomyces cerevisiae
R48A/W51A/H52A site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme Saccharomyces cerevisiae
R48L/W51L/H52L site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme Saccharomyces cerevisiae
R48V/W51V/H52V site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
cyanide cyanide binding can act as a surrogate for the hydrogen peroxide reaction. Structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron, equilibrium dissociation constants of wild-type and mutant enzymes, and pH-independent equilibrium dissociation constants for the high- and low-affinity cyanide binding phases of the triple mutants, overview Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state and transient kinetics, stopped-flow kinetics at pH 4.0 and pH 8.0 at 0.10 M ionic strength, 25 °C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Iron heme iron Fe(III) Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferrocytochrome c + H2O2 Saccharomyces cerevisiae
-
2 ferricytochrome c + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography and dialysis Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferrocytochrome c + H2O2
-
Saccharomyces cerevisiae 2 ferricytochrome c + 2 H2O
-
?
2 ferrocytochrome c + H2O2 via intermediate compound I formation. The rate-limiting step in CcP compound I formation is the binding of hydrogen peroxide to the heme iron rather than the redox chemistry involved in compound I formation Saccharomyces cerevisiae 2 ferricytochrome c + 2 H2O
-
?
iso-1 ferrocytochrome c mutant C102T + H2O2
-
Saccharomyces cerevisiae iso-1 ferricytochrome c mutant C102T + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
CCP
-
Saccharomyces cerevisiae
cytochrome c peroxidase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
heme
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron Saccharomyces cerevisiae