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show all sequences of 1.14.13.B28

Identification of the rate-limiting step of the peroxygenase reactions catalyzed by the thermophilic cytochrome P450 from Sulfolobus tokodaii strain 7

Hayakawa, S.; Matsumura, H.; Nakamura, N.; Yohda, M.; Ohno, H.; FEBS J. 281, 1409-1416 (2014)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
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
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
a FeIII/FeII couple in the heme cofactor of cytochrome P-450
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
styrene + NADH + H+ + O2
Sulfurisphaera tokodaii
-
styrene epoxide + NAD+ + H2O
-
-
?
styrene + NADH + H+ + O2
Sulfurisphaera tokodaii 7
-
styrene epoxide + NAD+ + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sulfurisphaera tokodaii
Q972I2
-
-
Sulfurisphaera tokodaii 7
Q972I2
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
744870
Sulfurisphaera tokodaii
?
-
-
-
-
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
744870
Sulfurisphaera tokodaii 7
?
-
-
-
-
styrene + NADH + H+ + O2
-
744870
Sulfurisphaera tokodaii
styrene epoxide + NAD+ + H2O
-
-
-
?
styrene + NADH + H+ + O2
-
744870
Sulfurisphaera tokodaii 7
styrene epoxide + NAD+ + H2O
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Sulfurisphaera tokodaii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0087
-
Styrene
pH 7.5, 25C
Sulfurisphaera tokodaii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
first optimum
Sulfurisphaera tokodaii
10
-
second optimum
Sulfurisphaera tokodaii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
3
12
activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes
Sulfurisphaera tokodaii
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P-450
-
Sulfurisphaera tokodaii
heme
containing a FeIII/FeII couple
Sulfurisphaera tokodaii
NADH
-
Sulfurisphaera tokodaii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P-450
-
Sulfurisphaera tokodaii
heme
containing a FeIII/FeII couple
Sulfurisphaera tokodaii
NADH
-
Sulfurisphaera tokodaii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
a FeIII/FeII couple in the heme cofactor of cytochrome P-450
Sulfurisphaera tokodaii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
styrene + NADH + H+ + O2
Sulfurisphaera tokodaii
-
styrene epoxide + NAD+ + H2O
-
-
?
styrene + NADH + H+ + O2
Sulfurisphaera tokodaii 7
-
styrene epoxide + NAD+ + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
744870
Sulfurisphaera tokodaii
?
-
-
-
-
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
744870
Sulfurisphaera tokodaii 7
?
-
-
-
-
styrene + NADH + H+ + O2
-
744870
Sulfurisphaera tokodaii
styrene epoxide + NAD+ + H2O
-
-
-
?
styrene + NADH + H+ + O2
-
744870
Sulfurisphaera tokodaii 7
styrene epoxide + NAD+ + H2O
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Sulfurisphaera tokodaii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0087
-
Styrene
pH 7.5, 25C
Sulfurisphaera tokodaii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
first optimum
Sulfurisphaera tokodaii
10
-
second optimum
Sulfurisphaera tokodaii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
3
12
activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes
Sulfurisphaera tokodaii
General Information
General Information
Commentary
Organism
malfunction
the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions
Sulfurisphaera tokodaii
metabolism
styrene epoxidation via the peroxide shunt pathway
Sulfurisphaera tokodaii
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
General Information (protein specific)
General Information
Commentary
Organism
malfunction
the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions
Sulfurisphaera tokodaii
metabolism
styrene epoxidation via the peroxide shunt pathway
Sulfurisphaera tokodaii
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
Other publictions for EC 1.14.13.B28
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744870
Hayakawa
Identification of the rate-li ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
FEBS J.
281
1409-1416
2014
-
-
-
-
1
-
-
-
-
1
-
2
-
4
-
-
-
-
-
-
-
-
4
-
1
-
-
1
2
1
-
3
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
1
2
1
-
-
-
3
3
-
-
-
725874
Matsumura
Monooxygenation by a thermophi ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Metallomics
3
389-395
2011
-
-
1
1
1
-
-
4
-
-
1
-
-
4
-
-
1
1
-
-
-
-
4
-
1
-
-
4
1
-
-
2
-
-
-
-
-
1
2
1
1
-
-
-
-
4
-
-
1
-
-
-
-
1
-
-
-
-
4
-
1
-
-
4
1
-
-
-
-
-
-
-
-
-
748359
Oku
Structure and direct electroc ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
J. Inorg. Biochem.
98
1194-1199
2004
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-
1
1
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
1
-
1
1
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
1
-
1
1
-
-
-
-
-
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