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Enzyme Nomenclature
Information on EC 1.14.13.69 - alkene monooxygenase
Word Map on EC 1.14.13.69
- 1.14.13.69
-
epoxidation
- xanthobacter
-
vinyl
-
diiron
- ethene
- oxygenases
- rhodochrous
-
4-monooxygenase
- nocardia
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dinuclear
- propyne
- nocardioides
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nonheme
- corallinus
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methanotrophic
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epoxygenation
- epoxyethane
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epoxidase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.14.13.69
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RECOMMENDED NAME
GeneOntology No.
alkene monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
propene + NADH + H+ + O2 = 1,2-epoxypropane + NAD+ + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epoxidation
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oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
alkene,NADH:oxygen oxidoreductase
This bacterial binuclear non-heme iron enzyme is a multicomponent enzyme complex comprising an oxygenase, a reductase, and a Rieske-type ferredoxin. The enzyme from the bacterium Xanthobacter sp. strain Py2 contains an additional small protein of unknown function that is essential for activity. In general, the enzyme oxygenates C2 to C6 aliphatic alkenes, although enzymes from different organisms show different substrate range. With propene as substrate, the stereospecifity of the epoxypropane formed is 95% (R) and 5% (S).
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CAS REGISTRY NUMBER
COMMENTARY
63439-50-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B-276; enzyme is encoded by the linear plasmid pNC30; i.e. Nocardia corallina
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strain B-276, formerly Nocardia corallina, high expression of enzyme when grown with propene as sole carbon and energy source
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strain B-276, formerly Nocardia corallina, high expression of enzyme when grown with propene as sole carbon and energy source
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gene xamoA, oxygenase alpha subunit; strain Py2, gene xamoA
SwissProt
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
-
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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-
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
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?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
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enables the growth on propene as sole carbon and energy source
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?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
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enables the growth on propene as sole carbon and energy source
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-
?
trans-1,2-dichloroethylene + NADH + H+ + O2
2,3-dichlorooxirane + NAD+ + H2O
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?
trans-1,2-dichloroethylene + NADH + H+ + O2
2,3-dichlorooxirane + NAD+ + H2O
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?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
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?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
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?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
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?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
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?
additional information
?
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alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
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additional information
?
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ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
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additional information
?
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the enzyme is a three-component system encoded by the 4-gene operon amoABCD, which catalyzes the stereoselective epoxidation of aliphatic alkenes yielding primarily the R enantiomer
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additional information
?
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the enzyme is a three-component system encoded by the 4-gene operon amoABCD, which catalyzes the stereoselective epoxidation of aliphatic alkenes yielding primarily the R enantiomer
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additional information
?
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alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules
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additional information
?
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the enzyme catalyses the asymmetric epoxidation of a broad range of alkenes, stereo- and regioselectivity, residues Asn34 and Arg57 are involved, AMO requires a small catalytic coupling/effector protein, AamD, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
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constitutive enzyme
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-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
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?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
induction by propylene and propylene oxide and a variety of aliphatic and chlorinated alkenes and epoxides
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
the inducible enzyme is central to the bacterial metabolism of aliphatic alkenes. Enzyme is expressed during growth of Xanthobacter on aliphatic alkenes or epoxides and repressed during growth on other carbon sources
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
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enables the growth on propene as sole carbon and energy source
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-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
enables the growth on propene as sole carbon and energy source
-
-
?
additional information
?
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alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
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-
-
additional information
?
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-
ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
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-
additional information
?
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alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme contains a Rieske-type ferredoxin. AMO requires a small catalytic coupling/effector protein, AamD, the coupling protein cannot or very poorly be substituted by coupling proteins of AMOs of other species, e.g. IsoD from Rhodococcus sp. strain AD45, or PmoB from Mycobacterium sp. strain M156, substitution with IsoD changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview
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FAD
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the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
[2Fe-2S]cluster
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the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation
Iron
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the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation
Iron
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the enzyme possesses a dinuclear iron center within the large subunit of the epoxygenase component, AmoC, mutagenesis of AmoC alters the enantioselectivity of the enzyme
Iron
the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin
Iron
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alpha-helical structure that surrounds the binuclear iron binding site
Iron
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enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, 2. a 13300 Da ferredoxin containing a Rieske-type 2Fe-2S cluster, 3. a 11000 Da monomeric protein that contains no detectable cofactors, 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron. The physiological electron acceptor for the reductase is the Rieske-type ferredoxin, which is proposed to be an intermediate electron carrier between the reductase and terminal catalytic component of the system
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
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2 mM, 40% inhibition. Activity is completely restored by 2 mM Fe2+
Ethyne
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irreversible inhibition in the presence of NADH, suicide substrate, growth inhibition when added to the culture medium
propyne
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irreversible inhibition in the presence of NADH, suicide substrate, growth inhibition when added to the culture medium
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AamD
the enzyme requires interaction with the small catalytic coupling/effector protein, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling
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additional information
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epoxyethane, a metabolic intermediate of ethene biodegradation, induces enzyme expression, acetate reactivates extant AkMO in starved vinyl chloride- or ethene-grown cultures, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
strain JS614 grows on the C2 alkenes ethene, vinyl chloride, and vinyl fluoride as sole carbon sources. The presence of 400-800 microM ethene oxide extended the growth substrate range to propene and butene. Propene-dependent growth of JS614 is CO2-dependent and is prevented by the carboxylase/reductase inhibitor 2-bromoethanesulfonic acid, while growth on ethene is not CO2-dependent or 2-bromoethanesulfonic acid-sensitive. Propene oxide at 0.05-0.1 mM exerts inhibitory effects on growth of JS614 on both acetate and ethene, and on ethene oxide-induced growth on ethene
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9650
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alpha2beta2gamma2, 2 * 58100, 2 * 38000, 2 * 9650, calculated from deduced amino acid sequences, masses in SDS-PAGE appear to be smaller (alpha and gamma subunits) or larger (beta subunit)
9740
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x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
11193
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x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
13359
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x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
34171
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x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
38000
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alpha2beta2gamma2, 2 * 58100, 2 * 38000, 2 * 9650, calculated from deduced amino acid sequences, masses in SDS-PAGE appear to be smaller (alpha and gamma subunits) or larger (beta subunit)
58037
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x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
58100
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alpha2beta2gamma2, 2 * 58100, 2 * 38000, 2 * 9650, calculated from deduced amino acid sequences, masses in SDS-PAGE appear to be smaller (alpha and gamma subunits) or larger (beta subunit)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
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alpha2beta2gamma2, 2 * 58100, 2 * 38000, 2 * 9650, calculated from deduced amino acid sequences, masses in SDS-PAGE appear to be smaller (alpha and gamma subunits) or larger (beta subunit)
additional information
additional information
the enzyme contains NADH-oxidoreductase and a Rieske-type ferredoxin components and the binuclear non-haem iron active site, it requires a small catalytic coupling/effector protein, AamD
additional information
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multi-component enzyme; x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
additional information
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enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, mass spectrometry 2. a dimeric ferredoxin consisting of two 13300 Da subunits, each containing a Rieske-type 2Fe-2S cluster, SDS-PAGE 3. a 11000 Da monomeric protein that contains no detectable cofactors, mass spectrometry 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron
additional information
-
enzyme contains 4 components: 1. a monomeric 35500 Da NADH reductase containing 1 mol of FAD and a probable 2Fe-2S center, mass spectrometry 2. a dimeric ferredoxin consisting of two 13300 Da subunits, each containing a Rieske-type 2Fe-2S cluster, SDS-PAGE 3. a 11000 Da monomeric protein that contains no detectable cofactors, mass spectrometry 4. a 212000 Da alpha2beta2gamma2 multimeric protein containing 4 atoms of nonheme iron; multi-component enzyme; x * 58037, oxygenase alpha-subunit, + x * 9740, gamma-subunit, + x * 13359, ferredoxin, + x * 11193, coupling or effector protein, + 38188, oxygenase beta-subunit, + x * 34171, reductase subunit, calculation from nucleotide sequence
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene etnC, expression analysis under different culture conditions, overview
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native and His-tagged protein expressed in Escherichia coli Rosetta(DE3)(pLysS)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both propene and propene oxide induce expression of the gene encoding the alpha subunit of alkene monooxygenase, etnC, to a similar level as ethene and ethene oxide
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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quasi random mutation of the large subunit of the epoxygenase component, AmoC alters the enantioselectivity of the enzyme, screening for altered epoxidation abilities
additional information
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quasi random mutation of the large subunit of the epoxygenase component, AmoC alters the enantioselectivity of the enzyme, screening for altered epoxidation abilities
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.69)
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