Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Saccharomyces cerevisiae |
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 | 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 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 | Comment | Organism | Structure |
---|---|---|---|
Iron | heme iron Fe(III) | Saccharomyces cerevisiae |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography and dialysis | Saccharomyces cerevisiae |
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 | Comment | Organism |
---|---|---|
CCP | - |
Saccharomyces cerevisiae |
cytochrome c peroxidase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Saccharomyces cerevisiae |
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 |