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Literature summary extracted from
- Identification of the rate-limiting step of the peroxygenase reactions catalyzed by the thermophilic cytochrome P450 from Sulfolobus tokodaii strain 7 (2014), FEBS J., 281, 1409-1416 .
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.11.2.1 | F310A/A320Q | site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s | Sulfurisphaera tokodaii |
| 1.14.13.B28 | F310A/A320Q | site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s | Sulfurisphaera tokodaii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.11.2.1 | 23.2 | - |
ethylbenzene | pH 5.0, 25°C | Sulfurisphaera tokodaii |  |
| 1.11.2.1 | 26.2 | - |
ethylbenzene | pH 10.0, 25°C | Sulfurisphaera tokodaii | |
| 1.11.2.1 | 81.4 | - |
ethylbenzene | pH 7.0, 25°C | Sulfurisphaera tokodaii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.2.1 | Iron | a FeIII/FeII couple in the heme cofactor of cytochrome P-450 | Sulfurisphaera tokodaii | |
| 1.14.13.B28 | Iron | a FeIII/FeII couple in the heme cofactor of cytochrome P-450 | Sulfurisphaera tokodaii | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.2.1 | ethylbenzene + H2O2 | Sulfurisphaera tokodaii | - |
1-phenylethanol + H2O | - |
? | |
| 1.11.2.1 | ethylbenzene + H2O2 | Sulfurisphaera tokodaii 7 | - |
1-phenylethanol + H2O | - |
? | |
| 1.14.13.B28 | styrene + NADH + H+ + O2 | Sulfurisphaera tokodaii | - |
styrene epoxide + NAD+ + H2O | - |
? | |
| 1.14.13.B28 | styrene + NADH + H+ + O2 | Sulfurisphaera tokodaii 7 | - |
styrene epoxide + NAD+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.2.1 | Sulfurisphaera tokodaii | Q972I2 | - |
- |
| 1.11.2.1 | Sulfurisphaera tokodaii 7 | Q972I2 | - |
- |
| 1.14.13.B28 | Sulfurisphaera tokodaii | Q972I2 | - |
- |
| 1.14.13.B28 | Sulfurisphaera tokodaii 7 | Q972I2 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.11.2.1 | RH + H2O2 = ROH + H2O | kinetic mechanism, overview | Sulfurisphaera tokodaii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.2.1 | ethylbenzene + H2O2 | - |
Sulfurisphaera tokodaii | 1-phenylethanol + H2O | - |
? | |
| 1.11.2.1 | ethylbenzene + H2O2 | - |
Sulfurisphaera tokodaii 7 | 1-phenylethanol + H2O | - |
? | |
| 1.11.2.1 | additional information | the enzyme catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation, as well as styrene epoxidation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant | Sulfurisphaera tokodaii | ? | - |
? | |
| 1.11.2.1 | additional information | the enzyme catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation, as well as styrene epoxidation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant | Sulfurisphaera tokodaii 7 | ? | - |
? | |
| 1.14.13.B28 | additional information | the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant | Sulfurisphaera tokodaii | ? | - |
? | |
| 1.14.13.B28 | additional information | the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant | Sulfurisphaera tokodaii 7 | ? | - |
? | |
| 1.14.13.B28 | styrene + NADH + H+ + O2 | - |
Sulfurisphaera tokodaii | styrene epoxide + NAD+ + H2O | - |
? | |
| 1.14.13.B28 | styrene + NADH + H+ + O2 | - |
Sulfurisphaera tokodaii 7 | styrene epoxide + NAD+ + H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.2.1 | P450st | - |
Sulfurisphaera tokodaii |
| 1.14.13.B28 | P450st | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.11.2.1 | 25 | - |
assay at | Sulfurisphaera tokodaii |
| 1.14.13.B28 | 25 | - |
assay at | Sulfurisphaera tokodaii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.11.2.1 | 0.0093 | - |
ethylbenzene | pH 5.0, 25°C | Sulfurisphaera tokodaii | |
| 1.11.2.1 | 0.125 | - |
ethylbenzene | pH 7.0, 25°C | Sulfurisphaera tokodaii | |
| 1.11.2.1 | 0.158 | - |
ethylbenzene | pH 10.0, 25°C | Sulfurisphaera tokodaii | |
| 1.14.13.B28 | 0.0087 | - |
Styrene | pH 7.5, 25°C | Sulfurisphaera tokodaii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.2.1 | 5 | - |
first optimum | Sulfurisphaera tokodaii |
| 1.11.2.1 | 10 | - |
second optimum | Sulfurisphaera tokodaii |
| 1.14.13.B28 | 5 | - |
first optimum | Sulfurisphaera tokodaii |
| 1.14.13.B28 | 10 | - |
second optimum | Sulfurisphaera tokodaii |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.2.1 | 3 | 12 | activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes | Sulfurisphaera tokodaii |
| 1.14.13.B28 | 3 | 12 | activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes | Sulfurisphaera tokodaii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.2.1 | cytochrome P450 | - |
Sulfurisphaera tokodaii | |
| 1.11.2.1 | heme | containing a FeIII/FeII couple | Sulfurisphaera tokodaii | |
| 1.11.2.1 | NADH | - |
Sulfurisphaera tokodaii | |
| 1.14.13.B28 | cytochrome P-450 | - |
Sulfurisphaera tokodaii | |
| 1.14.13.B28 | heme | containing a FeIII/FeII couple | Sulfurisphaera tokodaii | |
| 1.14.13.B28 | NADH | - |
Sulfurisphaera tokodaii | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.11.2.1 | malfunction | the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions | Sulfurisphaera tokodaii |
| 1.11.2.1 | metabolism | styrene epoxidation via the peroxide shunt pathway | Sulfurisphaera tokodaii |
| 1.11.2.1 | physiological function | cytochrome P450 from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 (P450st) is a thermophilic cytochrome P450 that shows high tolerance of harsh conditions and is capable of catalyzing some peroxygenase reactions. Both hydrogen peroxide-driven ethylbenzene hydroxylation and styrene epoxidation by wild-type P450st are found to be activated in weak acidic and weak basic solutions | Sulfurisphaera tokodaii |
| 1.14.13.B28 | malfunction | the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions | Sulfurisphaera tokodaii |
| 1.14.13.B28 | metabolism | styrene epoxidation via the peroxide shunt pathway | Sulfurisphaera tokodaii |
| 1.14.13.B28 | physiological function | cytochrome P450 from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 (P450st) is a thermophilic cytochrome P450 that shows high tolerance of harsh conditions and is capable of catalyzing some peroxygenase reactions. Both hydrogen peroxide-driven ethylbenzene hydroxylation and styrene epoxidation by wild-type P450st are found to be activated in weak acidic and weak basic solutions | Sulfurisphaera tokodaii |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.11.2.1 | 0.0004 | - |
ethylbenzene | pH 5.0, 25°C | Sulfurisphaera tokodaii | |
| 1.11.2.1 | 0.0015 | - |
ethylbenzene | pH 7.0, 25°C | Sulfurisphaera tokodaii | |
| 1.11.2.1 | 0.006 | - |
ethylbenzene | pH 10.0, 25°C | Sulfurisphaera tokodaii | |
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