Application | Comment | Organism |
---|---|---|
biotechnology | cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts | Saccharomyces cerevisiae |
Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of three apolar distal heme pocket mutants of CcP with enhanced binding of 1-methoxynaphthalene near the heme and enhanced hydroxylation activity of 1-methoxynaphthalene | Saccharomyces cerevisiae |
R48A/W51A/H52A | site-directed mutagenesis, the mutant shows 34fold higher activity with 1-methoxynaphthalene than the wild-type enzyme. While wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, mutant CcP is inactivated within four cycles of the peroxygenase reaction | Saccharomyces cerevisiae |
R48L/W51L/H52L | site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme | Saccharomyces cerevisiae |
R48V/W51V/H52V | site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Oxidation Stability | Organism |
---|---|
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-methoxynaphthalene + H2O2 | - |
Saccharomyces cerevisiae | Russig's blue + 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 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00007 | - |
1-methoxynaphthalene | pH 7.0, 25°C, wild-type enzyme | Saccharomyces cerevisiae | |
0.0022 | - |
1-methoxynaphthalene | pH 7.0, 25°C, mutant R48L/W51L/H52L | Saccharomyces cerevisiae | |
0.0023 | - |
1-methoxynaphthalene | pH 7.0, 25°C, mutant R48V/W51V/H52V | Saccharomyces cerevisiae | |
0.0025 | - |
1-methoxynaphthalene | pH 7.0, 25°C, mutant R48A/W51A/H52A | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction | Saccharomyces cerevisiae |