Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-styrene oxide + NADH + H+ + O2
?
-
-
-
?
(S)-styrene oxide + NADH + H+ + O2
?
-
-
-
?
1-butene + NADH + H+ + O2
2-ethyloxirane + NAD+ + H2O
1-octene + NADH + H+ + O2
2-hexyloxirane + NAD+ + H2O
-
-
-
-
?
2-cresol + NADH + H+ + O2
?
-
-
-
?
3-cresol + NADH + H+ + O2
?
-
-
-
?
4-cresol + NADH + H+ + O2
?
-
-
-
?
chloroethene + NADH + H+ + O2
2-chlorooxirane + NAD+ + H2O
ethene + NADH + H+ + O2
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
isoprene + NADH + H+ + O2
isoprene epoxide + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
styrene + NADH + H+ + O2
? + NAD+ + H2O
-
-
-
-
?
toluene + NADH + H+ + O2
?
-
-
-
?
trans-1,2-dichloroethylene + NADH + H+ + O2
2,3-dichlorooxirane + NAD+ + H2O
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
vinyl chloride + NADH + H+ + O2
?
additional information
?
-
1-butene + NADH + H+ + O2
2-ethyloxirane + NAD+ + H2O
-
-
-
-
?
1-butene + NADH + H+ + O2
2-ethyloxirane + NAD+ + H2O
-
best substrate
-
-
?
chloroethene + NADH + H+ + O2
2-chlorooxirane + NAD+ + H2O
-
-
-
-
?
chloroethene + NADH + H+ + O2
2-chlorooxirane + NAD+ + H2O
-
-
-
-
?
ethene + NADH + H+ + O2
?
-
-
-
-
?
ethene + NADH + H+ + O2
?
-
-
-
-
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
-
-
-
-
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
-
high activity
-
-
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
constitutive enzyme
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
constitutive enzyme
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
best substrate
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
best substrate
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
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
-
-
-
?
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
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
?
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
-
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
enables the growth on propene as sole carbon and energy source
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
enables the growth on propene as sole carbon and energy source
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
trans-1,2-dichloroethylene + NADH + H+ + O2
2,3-dichlorooxirane + NAD+ + H2O
-
-
-
-
?
trans-1,2-dichloroethylene + NADH + H+ + O2
2,3-dichlorooxirane + NAD+ + H2O
-
-
-
-
?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
-
-
-
-
?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
-
-
-
-
?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
-
-
-
-
?
trichloroethylene + NADH + H+ + O2
2,2,3-trichlorooxirane + NAD+ + H2O
-
-
-
-
?
vinyl chloride + NADH + H+ + O2
?
-
-
-
-
?
vinyl chloride + NADH + H+ + O2
?
-
-
-
-
?
additional information
?
-
-
EtnABCD is specialized for the oxidation of gaseous alkenes (C2 to C4), and its activity is much lower on liquid alkenes (C5 to C8), substrate specificity, overview. Cyclopentene and styrene are poor substrates
-
-
-
additional information
?
-
-
PmoABCD is specialized for the oxidation of gaseous alkenes (C2 to C4), and its activity is much lower on liquid alkenes (C5 to C8), substrate specificity, overview. Cyclopentene is a poor substrate
-
-
-
additional information
?
-
-
EtnABCD is specialized for the oxidation of gaseous alkenes (C2 to C4), and its activity is much lower on liquid alkenes (C5 to C8), substrate specificity, overview. Cyclopentene and styrene are poor substrates
-
-
-
additional information
?
-
-
PmoABCD is specialized for the oxidation of gaseous alkenes (C2 to C4), and its activity is much lower on liquid alkenes (C5 to C8), substrate specificity, overview. Cyclopentene is a poor substrate
-
-
-
additional information
?
-
-
alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
-
-
?
additional information
?
-
-
ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
-
-
?
additional information
?
-
-
alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
-
-
?
additional information
?
-
-
ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
product identification after reaction of th recombinant enzyme with isoprene by GC-MS
-
-
-
additional information
?
-
-
alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules
-
-
?
additional information
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ethene + NADH + H+ + O2
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
isoprene + NADH + H+ + O2
isoprene epoxide + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
vinyl chloride + NADH + H+ + O2
?
additional information
?
-
ethene + NADH + H+ + O2
?
-
-
-
-
?
ethene + NADH + H+ + O2
?
-
-
-
-
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
-
-
-
-
?
ethene + NADH + H+ + O2
oxirane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
constitutive enzyme
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
constitutive enzyme
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
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
-
enables the growth on propene as sole carbon and energy source
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
enables the growth on propene as sole carbon and energy source
-
-
?
propene + NADH + O2
1,2-epoxypropane + NAD+ + H2O
-
-
-
-
?
vinyl chloride + NADH + H+ + O2
?
-
-
-
-
?
vinyl chloride + NADH + H+ + O2
?
-
-
-
-
?
additional information
?
-
-
alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
-
-
?
additional information
?
-
-
ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
-
-
?
additional information
?
-
-
alkene monooxygenase and epoxyalkane:coenzyme M transferase are the initial enzymes of vinyl chloride and ethene biodegradation in strain JS614
-
-
?
additional information
?
-
-
ethene and propene are transformed by ethene-grown and propene-grown/EtO-induced JS614 to ethene oxide and propene oxide, respectively
-
-
?
additional information
?
-
-
alternative alkene cleavage mechanism by incorporating 2 oxygen atoms of different oxygen molecules
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
the endogenous IsoF component may be required to restore activity
evolution
-
isoprene monooxygenase (IsoMO) is a soluble diiron center monooxygenase in the same family of oxygenases as soluble methane monooxygenase, alkene monooxygenase, and toluene monooxygenase
evolution
-
the enzyme belongs to the bacterial monooxygenases of the soluble di-iron MOs (SDIMOs) type, thereof the group 4 SDIMOs are four-component alkene monooxygenases from bacteria that grow on ethene and/or propene. Despite their sequence and substrate diversity, all the SDIMOs have similar biochemistries. Electrons are transferred from NADH to an oxidoreductase protein that contains flavin and iron-sulfur clusters, and thence to a catalytic hydroxylase (made of 2 to 3 proteins) that contains the binuclear iron active site. In the active site, one oxygen atom in O2 is reduced to water, while the other is activated to a high-energy state and attacks the substrate. The catalytic activity is acilitated by a small cofactor-independent coupling protein, and depending on the SDIMO family, other proteins, such as ferredoxins, may also be part of the MO-enzyme complex. Mycobacterium chubuense NBB4 is unique among hydrocarbon-oxidizing bacteria because it contains four different SDIMOs, in addition to a copper-containing MO, a P450, and an alkB homologue. Strain NBB4 has two group 4 SDIMOs (etnABCD and pmoABCD), an atypical group 3 SDIMO (smoXYB1C1Z), and a group 6 SDIMO (smoABCD). To date, there is experimental evidence that smoXYB1C1Z is a gaseous alkane/alkene MO and that etnABCD is an ethene MO. Comparison of SDIMO activities in whole cells of wild-type and recombinant bacteria, overview
evolution
-
the enzyme belongs to the bacterial monooxygenases of the soluble di-iron MOs (SDIMOs) type, thereof the group 4 SDIMOs are four-component alkene monooxygenases from bacteria that grow on ethene and/or propene. Despite their sequence and substrate diversity, all the SDIMOs have similar biochemistries. Electrons are transferred from NADH to an oxidoreductase protein that contains flavin and iron-sulfur clusters, and thence to a catalytic hydroxylase (made of 2 to 3 proteins) that contains the binuclear iron active site. In the active site, one oxygen atom in O2 is reduced to water, while the other is activated to a high-energy state and attacks the substrate. The catalytic activity is acilitated by a small cofactor-independent coupling protein, and depending on the SDIMO family, other proteins, such as ferredoxins, may also be part of the MO-enzyme complex. Mycobacterium chubuense NBB4 is unique among hydrocarbon-oxidizing bacteria because it contains four different SDIMOs, in addition to a copper-containing MO, a P450, and an alkB homologue. Strain NBB4 has two group 4 SDIMOs (etnABCD and pmoABCD), an atypical group 3 SDIMO (smoXYB1C1Z), and a group 6 SDIMO (smoABCD). To date, there is experimental evidence that smoXYB1C1Z is a gaseous alkane/alkene MO and that etnABCD is an ethene MO. Comparison of SDIMO activities in whole cells of wild-type and recombinant bacteria, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11193
-
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
-
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
-
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
-
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
-
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
-
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)
9650
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hexamer
-
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)
heterotetramer
-
1 * 36000, subunit EtnA, + 1 * 12000 subunit EtnB, + 1 * 59000, subunit EtnC, + 1 * 37000, subunit EtnD, SDS-PAGE
heterotetramer
-
1 * 39000, subunit PmoA, + 1 * 12000 subunit PmoB, + 1 * 57000, subunit PmoC, + 1 * 37000, subunit PmoD, SDS-PAGE
heterotetramer
-
1 * 36000, subunit EtnA, + 1 * 12000 subunit EtnB, + 1 * 59000, subunit EtnC, + 1 * 37000, subunit EtnD, SDS-PAGE
-
heterotetramer
-
1 * 39000, subunit PmoA, + 1 * 12000 subunit PmoB, + 1 * 57000, subunit PmoC, + 1 * 37000, subunit PmoD, SDS-PAGE
-
additional information
-
multi-component enzyme
additional information
-
multi-component enzyme
-
additional information
-
multi-component enzyme
additional information
-
multi-component enzyme
-
additional information
-
multi-component enzyme
additional information
-
multi-component enzyme
-
additional information
-
the alkene MO consists of a small hydroxylase subunit EtnA of 36 kDa, a coupling protein subunit EtnB of12 kDa, a large hydroxylase subunit EtnC of 59 kDa, and a reductase subunit EtnD of 37 kDa
additional information
-
the alkene MO consists of a small hydroxylase subunit PmoA of 39 kDa, a coupling protein subunit PmoB of12 kDa, a large hydroxylase subunit PmoC of 57 kDa, and a reductase subunit PmoD of 37 kDa
additional information
-
the alkene MO consists of a small hydroxylase subunit EtnA of 36 kDa, a coupling protein subunit EtnB of12 kDa, a large hydroxylase subunit EtnC of 59 kDa, and a reductase subunit EtnD of 37 kDa
-
additional information
-
the alkene MO consists of a small hydroxylase subunit PmoA of 39 kDa, a coupling protein subunit PmoB of12 kDa, a large hydroxylase subunit PmoC of 57 kDa, and a reductase subunit PmoD of 37 kDa
-
additional information
-
the four component IsoMO is likely to comprise an oxygenase (IsoABE), reductase (IsoF), coupling protein (IsoD) and Rieske-type ferredoxin (IsoC). The alpha subunit of the oxygenase component of SDIMOs (equivalent to IsoA in IsoMO) contains an active site diiron center required for catalytic activity of the enzyme. The oxygenase component might form dimers in an (alphabetagamma)2 arrangement. The beta subunit (IsoE) and the gamma subunit (IsoB) combine with the alpha subunit to form the oxygenase complex
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
-
multi-component enzyme
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
additional information
-
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
-
multi-component enzyme
-
additional information
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Habets-Cruetzen, A.Q.H.; De Bont, J.A.M.
Inactivation of alkene oxidation by epoxides in alkene- and alkane-grown bacteria
Appl. Microbiol. Biotechnol.
22
428-433
1985
Mycobacterium sp., Mycobacterium sp. E20, Mycobacterium sp. E3
-
brenda
Gallagher, S.C.; Cammack, R.; Dalton, H.
Electron transfer reactions in the alkene mono-oxygenase complex from Nocardia corallina B-276
Biochem. J.
339
79-85
1999
Gordonia rubripertincta, Gordonia rubripertincta B-276
brenda
Ensign, S.A.
Aliphatic and chlorinated alkenes and epoxides as inducers of alkene monooxygenase and epoxidase activities in Xanthobacter strain Py2
Appl. Environ. Microbiol.
62
61-66
1996
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Gallagher, S.C.; Cammack, R.; Dalton, H.
Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions
Eur. J. Biochem.
247
635-641
1997
Gordonia rubripertincta, Gordonia rubripertincta B-276
brenda
Saeki, H.; Akira, M.; Furuhashi, K.; Averhoff, B.; Gottschalk, G.
Degradation of trichloroethene by a linear-plasmid-encoded alkene monooxygenase in Rhodococcus corallinus (Nocardia corallina) B-276
Microbiology
145
1721-1730
1999
Gordonia rubripertincta, Rhodococcus ruber, Xanthobacter sp., Gordonia rubripertincta B-276, Xanthobacter sp. Py2
brenda
Zhou, N.Y.; Jenkins, A.; Chan Kwo Chion, C.K.N.; Leak, D.J.
The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-heme iron protein closely related to toluene 4-monooxygenase
FEBS Lett.
430
181-185
1998
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Hartmans, S.; Weber, F.J.; Somhorst, D.P.M.; De Bont, J.A.M.
Alkene monooxygenase from Mycobacterium: a multicomponent enzyme
J. Gen. Microbiol.
137
2555-2560
1991
Mycobacterium sp., Mycolicibacterium aurum, Mycobacterium sp. E3, Mycolicibacterium aurum L1
brenda
Zhou, N.Y.; Jenkins, A.; Chan Kwo Chion, C.K.; Leak, D.J.
The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol
Appl. Environ. Microbiol.
65
1589-1595
1999
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Small, F.J.; Ensign, S.A.
Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes
J. Biol. Chem.
272
24913-24920
1997
Xanthobacter sp., Xanthobacter sp. Py2
brenda
Zhou, N.Y.; Chan Kwo Chion, C.K.N.; Leak, D.J.
Cloning and expression of the genes encoding propene monooxygenase from Xanthobacter Py2
Appl. Microbiol. Biotechnol.
44
582-588
1996
Xanthobacter sp., Xanthobacter sp. Py2
-
brenda
Fosdike, W.L.; Smith, T.J.; Dalton, H.
Adventitious reactions of alkene monooxygenase reveal common reaction pathways and component interactions among bacterial hydrocarbon oxygenases
FEBS J.
272
2661-2669
2005
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
brenda
Champreda, V.; Zhou, N.Y.; Leak, D.J.
Heterologous expression of alkene monooxygenase components from Xanthobacter autotrophicus Py2 and reconstitution of the active complex
FEMS Microbiol. Lett.
239
309-318
2004
Xanthobacter autotrophicus
brenda
Champreda, V.; Choi, Y.J.; Zhou, N.Y.; Leak, D.J.
Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions
Appl. Microbiol. Biotechnol.
71
840-847
2006
Xanthobacter autotrophicus (O87082)
brenda
Perry, A.; Smith, T.J.
Protocol for mutagenesis of alkene monooxygenase and screening for modified enantiocomposition of the epoxypropane product
J. Biomol. Screen.
11
553-556
2006
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
brenda
Mattes, T.E.; Coleman, N.V.; Chuang, A.S.; Rogers, A.J.; Spain, J.C.; Gossett, J.M.
Mechanism controlling the extended lag period associated with vinyl chloride starvation in Nocardioides sp. strain JS614
Arch. Microbiol.
187
217-226
2007
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499
brenda
Lara, M.; Mutti, F.; Glueck, S.; Kroutil, W.
Oxidative enzymatic alkene cleavage: Indications for a nonclassical enzyme mechanism
J. Am. Chem. Soc.
131
5368-5369
2009
Trametes hirsuta
brenda
Chuang, A.; Jin, Y.; Schmidt, L.; Li, Y.; Fogel, S.; Smoler, D.; Mattes, T.
Proteomic analysis of ethene-enriched groundwater microcosms from a vinyl chloride-contaminated site
Environ. Sci. Technol.
44
1594-1601
2010
Nocardioides sp. JS614
brenda
Taylor, A.E.; Arp, D.J.; Bottomley, P.J.; Semprini, L.
Extending the alkene substrate range of vinyl chloride utilizing Nocardioides sp. strain JS614 with ethene oxide
Appl. Microbiol. Biotechnol.
87
2293-2302
2010
Nocardioides sp., Nocardioides sp. JS614 / ATCC BAA-499
brenda
Saitoh, S.; Aoyama, H.; Akutsu, M.; Nakano, K.; Shinzato, N.; Matsui, T.
Genomic sequencing-based detection of large deletions in Rhodococcus rhodochrous strain B-276
J. Biosci. Bioeng.
116
309-312
2013
Rhodococcus rhodochrous, Rhodococcus rhodochrous B-276
brenda
McCarl, V.; Somerville, M.V.; Ly, M.A.; Henry, R.; Liew, E.F.; Wilson, N.L.; Holmes, A.J.; Coleman, N.V.
Heterologous expression of Mycobacterium alkene monooxygenases in Gram-positive and Gram-negative bacterial hosts
Appl. Environ. Microbiol.
84
e00397-18
2018
Mycolicibacterium chubuense, Mycolicibacterium chubuense NBB4
brenda
Sims, L.P.; Lockwood, C.W.J.; Crombie, A.T.; Bradley, J.M.; Le Brun, N.E.; Murrell, J.C.
Purification and characterization of the isoprene monooxygenase from Rhodococcus sp. strain AD45
Appl. Environ. Microbiol.
88
e0002922
2022
Rhodococcus sp. AD45
brenda