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Information on EC 1.14.13.B28 - monooxygenase CYP119A2 and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q972I2

for references in articles please use BRENDA:EC1.14.13.B28
preliminary BRENDA-supplied EC number
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Sulfurisphaera tokodaii
UNIPROT: Q972I2
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Word Map
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The expected taxonomic range for this enzyme is: Sulfolobaceae
Reaction Schemes
Synonyms
cytochrome p450 119, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytochrome P450 119
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
show the reaction diagram
sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released
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
the initial rate of catalysis with NADH is slightly higher than with NADPH
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
-
-
NADPH
the initial rate of catalysis with NADH is slightly higher than with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 12
activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
a clear redox response is observed at even 80°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions
metabolism
styrene epoxidation via the peroxide shunt pathway
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
F-G loop deletion mutant enzyme delLL151-E156
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method using a protein solution (15 mg/ml) and a reservoir solution (30% (w/v) polyethylene glycol 4000, 200 mM lithium sulfate monohydrate and 100 mM Tris-HCl, pH 8.5)
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
delL151-E156
the Km value of the mutant is about 2times lower than that of the wild-type.
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsumura, H.; Matsuda, K.; Nakamura, N.; Ohtaki, A.; Yoshida, H.; Kamitori, S.; Yohda, M.; Ohno, H.
Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH
Metallomics
3
389-395
2011
Sulfurisphaera tokodaii (Q972I2), Sulfurisphaera tokodaii 7 (Q972I2)
Manually annotated by BRENDA team
Hayakawa, S.; Matsumura, H.; Nakamura, N.; Yohda, M.; Ohno, H.
Identification of the rate-limiting step of the peroxygenase reactions catalyzed by the thermophilic cytochrome P450 from Sulfolobus tokodaii strain 7
FEBS J.
281
1409-1416
2014
Sulfurisphaera tokodaii (Q972I2), Sulfurisphaera tokodaii 7 (Q972I2)
Manually annotated by BRENDA team
Oku, Y.; Ohtaki, A.; Kamitori, S.; Nakamura, N.; Yohda, M.; Ohno, H.; Kawarabayasi, Y.
Structure and direct electrochemistry of cytochrome P450 from the thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7
J. Inorg. Biochem.
98
1194-1199
2004
Sulfurisphaera tokodaii (Q972I2), Sulfurisphaera tokodaii 7 (Q972I2)
Manually annotated by BRENDA team