Information on EC 1.14.14.11 - styrene monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.11
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RECOMMENDED NAME
GeneOntology No.
styrene monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
styrene + FADH2 + O2 = (S)-2-phenyloxirane + FAD + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epoxidation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
styrene degradation
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Styrene degradation
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
styrene,FADH2:oxygen oxidoreductase
The enzyme catalyses the first step in the aerobic styrene degradation pathway. It forms a two-component system with a reductase (StyB) that utilizes NADH to reduce flavin-adenine dinucleotide, which is then transferred to the oxygenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1E)-prop-1-en-1-ylbenzene + FADH2 + O2
(2R,3S)-2-methyl-3-phenyloxirane + FAD + H2O
show the reaction diagram
(2E)-3-phenylprop-2-en-1-ol + FADH2 + O2
(3-phenyloxiran-2-yl)methanol + 1-phenylpropane-1,2,3-triol + FAD + H2O
show the reaction diagram
(2E)-3-phenylprop-2-en-1-yl acetate + FADH2 + O2
(3-phenyloxiran-2-yl)methyl acetate + 2,3-dihydroxy-3-phenylpropyl acetate + FAD + H2O
show the reaction diagram
1,2-dihydronaphthalene + FADH2 + O2
(1R,2R)-1,2,3,4-tetrahydronaphthalene-1,2-diol + FAD + H2O
show the reaction diagram
1,2-dihydronaphthalene + FADH2 + O2
(1R,2R)-1,2-dihydronaphthalene-1,2-diol + FAD + H2O
show the reaction diagram
1-hexene + FADH2 + O2
?
show the reaction diagram
1-octene + FADH2 + O2
?
show the reaction diagram
1H-indene + FADH2 + O2
(1aS,6aR)-6,6a-dihydro-1aH-indeno[1,2-b]oxirene + FAD + H2O
show the reaction diagram
2-bromothioanisole + FADH2 + O2
?
show the reaction diagram
2-chlorostyrene + FADH2 + O2
(2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
show the reaction diagram
2-chlorostyrene + FADH2 + O2
?
show the reaction diagram
2-chlorothioanisole + FADH2 + O2
?
show the reaction diagram
2-ethenylpyridine + FADH2 + O2
2-(oxiran-2-yl)pyridine + FAD + H2O
show the reaction diagram
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-
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?
2-ethylstyrene + FADH2 + O2
(S)-2-ethyl-2-phenyloxirane + FAD + H2O
show the reaction diagram
2-methylbenzo[b]thiophene + FADH2 + O2
?
show the reaction diagram
2-methylstyrene + FADH2 + O2
(S)-2-methyl-2-phenyloxirane + FAD + H2O
show the reaction diagram
2-methylthioanisole + FADH2 + O2
?
show the reaction diagram
3-chlorostyrene + FADH2 + O2
(2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
show the reaction diagram
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-
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?
3-chlorostyrene + FADH2 + O2
(2S)-3-(3-chlorophenyl)oxirane + FAD + H2O
show the reaction diagram
3-chlorostyrene + FADH2 + O2
?
show the reaction diagram
3-methylstyrene + FADH2 + O2
(2S)-2-(3-methylphenyl)oxirane + FAD + H2O
show the reaction diagram
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-
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?
4-bromostyrene + FADH2 + O2
(2S)-2-(4-bromophenyl)oxirane + FAD + H2O
show the reaction diagram
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-
-
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?
4-bromostyrene + FADH2 + O2
?
show the reaction diagram
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?
4-bromothioanisole + FADH2 + O2
?
show the reaction diagram
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-
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?
4-chlorostyrene + FADH2 + O2
(2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
show the reaction diagram
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-
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?
4-chlorostyrene + FADH2 + O2
(2S)-4-(4-chlorophenyl)oxirane + FAD + H2O
show the reaction diagram
4-chlorostyrene + FADH2 + O2
?
show the reaction diagram
4-chlorothioanisole + FADH2 + O2
?
show the reaction diagram
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-
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?
4-ethenylpyridine + FADH2 + O2
4-(oxiran-2-yl)pyridine + FAD + H2O
show the reaction diagram
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-
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?
4-fluorostyrene + FADH2 + O2
(2S)-2-(4-fluorophenyl)oxirane + FAD + H2O
show the reaction diagram
-
-
-
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?
4-fluorostyrene + FADH2 + O2
?
show the reaction diagram
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?
4-methylstyrene + FADH2 + O2
(2S)-2-(4-methylphenyl)oxirane + FAD + H2O
show the reaction diagram
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?
4-methylstyrene + FADH2 + O2
? + FAD + H2O
show the reaction diagram
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?
4-methylthioanisole + FADH2 + O2
?
show the reaction diagram
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?
allylbenzene + FADH2 + O2
?
show the reaction diagram
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?
benzo[b]thiophene + FADH2 + O2
benzo[b]thiophene sulfoxide + FAD + H2O
show the reaction diagram
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?
indene + FADH2 + O2
(1S,2R)-indene oxide + FAD + H2O
show the reaction diagram
indene + FADH2 + O2
indene 2,3-oxide + FAD + H2O
show the reaction diagram
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?
indole + FADH2 + O2
indole 2,3-oxide + FAD + H2O
show the reaction diagram
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?
indole+ FADH2 + O2
?
show the reaction diagram
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?
methyl (2E)-3-phenylprop-2-enoate + FADH2 + O2
methyl 3-phenyloxirane-2-carboxylate + methyl 2,3-dihydroxy-3-phenylpropanoate + FAD + H2O
show the reaction diagram
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?
naphthalene + FADH2 + O2
(1R,2R)-1,2-dihydronaphthalene-1,2-diol + FAD + H2O
show the reaction diagram
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trace amount
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?
prop-1-en-2-ylbenzene + FADH2 + O2
2-phenylpropane-1,2-diol + FAD + H2O
show the reaction diagram
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?
styrene + FADH2 + O2
(S)-2-phenyloxirane + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
(S)-7,8-styrene oxide + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
(S)-styrene oxide + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
styrene oxide + FAD + H2O
show the reaction diagram
thioanisole + FADH2 + O2
?
show the reaction diagram
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best substrate
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?
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 + FADH2 + O2
(S)-2-phenyloxirane + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
(S)-7,8-styrene oxide + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
(S)-styrene oxide + FAD + H2O
show the reaction diagram
styrene + FADH2 + O2
styrene oxide + FAD + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
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the enzyme favors FAD and FMN over riboflavin; the enzyme favors FAD and FMN over riboflavin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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StyA does not contain Fe2+, Cu2+, Zn2+, Mn2+, Co2+, or Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-chlorostyrene
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less than 30% residual activity with 25 mM 3-chlorostyrene; less than 30% residual activity with 25 mM 3-chlorostyrene
Benzene
FAD
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at a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases
NaCl
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a salt concentration of 162 mM results in half of the maximum inhibitory effect
Styrene
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less than 40% residual activity with 5 mM styrene; less than 40% residual activity with 5 mM styrene
styrene oxide
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marked inhibition; marked inhibition
additional information
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not inhibited by 1-hexene; not inhibited by 1-hexene
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046 - 0.45
Styrene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
Styrene
Pseudomonas sp.
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pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0026
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cell-free extract, at pH 7.0 and 30°C
0.0114
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cell-free extract, at pH 7.0 and °C
0.0255
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after 2.2fold purification, at pH 7.0 and 30°C
0.0304
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after 11.7fold purification, at pH 7.0 and 30°C
1.9
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pH 7.5, 37°C, wild-type StyA
2.1
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pH 7.5, 37°C, recombinant StyA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59000
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gel filtration; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
catalytic activity of recombinant Escherichia coli is not stable and decreases with reaction time
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Sepabeads EC-EA and EC-Q1A anion-exchange carriers are employed to non-covalently adsorb StyA from the cell extracts. Sepabeads may be reused for several catalytic cycles without significant loss of enzyme, especially if immobilizations are carried out at pH 6
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, addition of 10% v/v glycerol and 1 mM pefabloc to the storage buffer improves enzyme stability, the activity decreases by 20% during the first 2 weeks, StyA retains 60% of its initial activity after 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminally histidine-tagged styrene monooxygenase
Ni-NTA affinity column chromatography
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Ni-Sepharose column chromatography and MonoQ column chromatography; Toyopearl SuperQ-650 M column chromatography, Ni-Sepharose column chromatography, MonoQ column chromatography and Superdex 200 gel filtration
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nickel-affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 pLysS cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli. 50% sequence identity with styrene monooxygenases from pseudomonads
expression in Pseudomonmas putida KT2440
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expression of mutant enzymes in Escherichia coli
expression of native and histidine-tagged versions of SMOA in Escherichia coli BL21
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functional expression of His10-StyA2B in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction/repression of the sty operon in Pseudomonas putida CA-3, during growth on phenylacetic acid under continuous culture conditions, involves regulatory mechanisms coordinately affecting both the upper and lower pathways and acting at the level of gene transcription
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L44A
mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
L45A
mutation leads to a change of substrate preference. The mutant enzyme exhibits a remarkably reversed substrate preference compared to the wild type, displaying increased reactivity with an increase in substrate size. The activity of L45A is about 5% of that of the wild type towards styrene, but reaches about 30 and about 90% when the substrate is changed to 2-methylstyrene and 2-ethylstyrene, respectively
N46A
mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
R43A
mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
L44A
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mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
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L45A
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mutation leads to a change of substrate preference. The mutant enzyme exhibits a remarkably reversed substrate preference compared to the wild type, displaying increased reactivity with an increase in substrate size. The activity of L45A is about 5% of that of the wild type towards styrene, but reaches about 30 and about 90% when the substrate is changed to 2-methylstyrene and 2-ethylstyrene, respectively
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N46A
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mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
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R43A
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mutation leads to a change of substrate preference, substrate preference for 2-methylstyrene
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T200V
mutant exhibits lower reactivity than the wild type, displayed impaired diastereoselectivity
Y73F
mutant exhibits lower reactivity than the wild type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis