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Literature summary for 1.11.1.5 extracted from
- Relocation of the distal histidine in cytochrome c peroxidase: properties of CcP(W51H), CcP(W51H/H52W), and CcP(W51H/H52L) (2009), Biochemistry, 48, 5417-5425.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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 |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cytochrome c + H2O2 | Saccharomyces cerevisiae | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
bakerยs yeast | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cytochrome c + H2O2 | - |
Saccharomyces cerevisiae | ? | - |
? | |
| 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 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCP | - |
Saccharomyces cerevisiae |
| cytochrome c peroxidase | - |
Saccharomyces cerevisiae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 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 |
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Release 2023.1 (January 2023)
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