Information on EC 1.14.13.B28 - monooxygenase CYP119A2

for references in articles please use BRENDA:EC1.14.13.B28
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The expected taxonomic range for this enzyme is: Sulfurisphaera tokodaii

EC NUMBER
COMMENTARY hide
1.14.13.B28
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
monooxygenase CYP119A2
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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styrene epoxidation via the peroxide shunt pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
show the reaction diagram
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
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-
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heme
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containing a FeIII/FeII couple
NADPH
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the initial rate of catalysis with NADH is slightly higher than with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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a FeIII/FeII couple in the heme cofactor of cytochrome P-450
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7 - 13
NADH
0.29 - 0.52
Styrene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000076 - 0.000079
NADH
0.000057 - 0.0087
Styrene
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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first optimum
10
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second optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 12
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activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
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F-G loop deletion mutant enzyme delLL151-E156
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method, X-ray crystallography at a resolution of 1.94 A reveals a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The mutant shows a higher affinity for NADH compared with the wild-type because the mutant has a more widely open distal pocket for NAD(P)H binding
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
delL151-E156
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the Km value of the mutant is about 2times lower than that of the wild-type.
F310A/A320Q
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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
delL151-E156
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the Km value of the mutant is about 2times lower than that of the wild-type.
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F310A/A320Q
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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
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