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Information on EC 1.14.13.B28 - monooxygenase CYP119A2
for references in articles please use BRENDA:EC1.14.13.B28
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.B28 monooxygenase CYP119A2
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
- 1.14.13.B28
-
lauric
- porphyrin
-
photolysis
-
kbind
-
benzyl
-
first-order
- flash
- sulfur
- peroxynitrite
-
ironiv-oxo
showSynonyms
cytochrome p450 119, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP119
cytochrome P450 119
P450st
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released
-
-
styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
styrene + cumene hydroperoxide
styrene epoxide + ?
-
Substrates: -
Products: -
Products: -
?
styrene + cumene hydroperoxide
styrene epoxide + ?
-
Substrates: -
Products: -
Products: -
?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: the initial rate of catalysis with NADH is slightly higher than with NADPH
Products: -
Products: -
?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: the initial rate of catalysis with NADH is slightly higher than with NADPH
Products: -
Products: -
?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
Substrates: the initial rate of catalysis with NADH is slightly higher than with NADPH
Products: -
Products: -
?
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
Substrates: the initial rate of catalysis with NADH is slightly higher than with NADPH
Products: -
Products: -
?
styrene + tert-butyl hydroperoxide
styrene epoxide + ?
-
Substrates: -
Products: -
Products: -
?
styrene + tert-butyl hydroperoxide
styrene epoxide + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the initial activities of CYP119 in the presence of tert-butyl hydroperoxide and cumene hydroperoxide are two- and fivefold higher than that observed with H2O2. tert-Butyl hydroperoxide increases both turnover rate and the stability of the enzyme under the oxidizing reaction conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the initial activities of CYP119 in the presence of tert-butyl hydroperoxide and cumene hydroperoxide are two- and fivefold higher than that observed with H2O2. tert-Butyl hydroperoxide increases both turnover rate and the stability of the enzyme under the oxidizing reaction conditions
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
the initial rate of catalysis with NADH is slightly higher than with NADPH
heme
electron-transfer reaction between the electrode and heme iron
heme
-
sequence contains the consensus heme-binding sequence Phe-Gly-Xaa-Gly-Xaa-His-Xaa-Cys-Xaa-Gly-Xaa3-Ala-Arg-Xaa-Glu
heme
-
substrate free oxidized form of the protein shows a Soret maximum at 415 nm and visible bands at 533 and 566 nm. In the reduced form the Soret band blue shifts to 410 nm
NADH
the initial rate of catalysis with NADH is slightly higher than with NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
a FeIII/FeII couple in the heme cofactor of cytochrome P-450
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
activity range, profile overview. Analysis of pH dependencies of wild-type and mutant enzymes
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions
malfunction
-
the F310A/A320Q mutant catalyzes styrene epoxidation via the peroxide shunt pathway more efficiently than wild-type P450st in neutral solutions
-
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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CP119_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
368
0
42863
Swiss-Prot
-
CP119_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
367
0
42324
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
exhibits remarkable thermo- and pressure stability, i.e. a hydrostatic pressure up to 2 kbar
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a heat denaturation step, ammonium sulfate precipitation (30-50%), a size exclusion column, and an HPLC anion exchange column
-
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
coexpression of 5-aminolevulinic acid synthase (ALAS) from Rhodobacter capsulatus improves the heterologous production of CYP119. Coexpression of ALAS increases the amount of heterologous CYP119 isolated and the ratio of its holo form. The ratio of holo-CYP119 resulting from the coexpression of ALAS in Escherichia coli is 99%, whereas that from cells expressing CYP119 exclusively is 66%
synthesis
-
coexpression of 5-aminolevulinic acid synthase (ALAS) from Rhodobacter capsulatus improves the heterologous production of CYP119. Coexpression of ALAS increases the amount of heterologous CYP119 isolated and the ratio of its holo form. The ratio of holo-CYP119 resulting from the coexpression of ALAS in Escherichia coli is 99%, whereas that from cells expressing CYP119 exclusively is 66%
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rabe, K.S.; Kiko, K.; Niemeyer, C.M.
Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius
Chembiochem
9
420-425
2008
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
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)
brenda
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)
brenda
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)
brenda
Honda, Y.; Nanasawa, K.; Fujii, H.
Coexpression of 5-aminolevulinic acid synthase gene facilitates heterologous production of thermostable cytochrome P450, CYP119, in holo form in Escherichia coli
ChemBioChem
19
2156-2159
2018
Sulfolobus acidocaldarius (Q55080), Sulfolobus acidocaldarius ATCC 33909 (Q55080)
brenda
McLean, M.A.; Maves, S.A.; Weiss, K.A.; Krepich, S.; Sligar, S.G.
Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus
Biochem. Biophys. Res. Commun.
252
166-172
1998
Saccharolobus solfataricus
brenda
Wright, R.L.; Harris, K.; Solow, B.; White, R.H.; Kennelly, P.J.
Cloning of a potential cytochrome P450 from the archaeon Sulfolobus solfataricus
FEBS Lett.
384
235-239
1996
Saccharolobus solfataricus
brenda
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