EC Number | Cloned (Comment) | Organism |
---|---|---|
1.11.1.5 | expression in Escherichia coli | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.11.1.5 | additional information | significant decreases in the rate of reaction with hydrogen peroxide with 56-, 300-, and 6200fold decreases for mutant (W51H), mutant (W51H/H52W), and mutant (W51H/H52L), respectively, compared to that of wild-type cytochrome c peroxidase, indicating that the position of the distal histidine has a significant effect on the rate of reaction with H2O2 | Saccharomyces cerevisiae |
1.11.1.5 | W51H | altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase | Saccharomyces cerevisiae |
1.11.1.5 | W51H/H52L | altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase | Saccharomyces cerevisiae |
1.11.1.5 | W51H/H52W | altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.11.1.5 | cyanide | the W51H mutations have a weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase. The cyanide association rate constants are between 5 and 85times slower for the W51H mutants, while the cyanide dissociation rate constants range from 3times slower to 6times faster than those of wild-type cytochrome c peroxidase | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.5 | cytochrome c + H2O2 | Saccharomyces cerevisiae | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.5 | Saccharomyces cerevisiae | - |
bakerยs yeast | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.11.1.5 | - |
Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.5 | cytochrome c + H2O2 | - |
Saccharomyces cerevisiae | ? | - |
? | |
1.11.1.5 | cytochrome c + H2O2 | the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.11.1.5 | CCP | - |
Saccharomyces cerevisiae |
1.11.1.5 | cytochrome c peroxidase | - |
Saccharomyces cerevisiae |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.11.1.5 | 4 | 8 | mutants W51H, W51H/H52W and W51H/H52L are significantly less stable at pH 4.0 than wild-type cytochrome c peroxidase, at pH 4, the Soret band of the spectra for all three mutants undergoes a loss of absorptivity, suggesting the beginning of acid denaturation | Saccharomyces cerevisiae |