1.14.13.69: alkene monooxygenase
This is an abbreviated version!
For detailed information about alkene monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.69
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1.14.13.69
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epoxidation
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xanthobacter
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vinyl
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diiron
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nocardioides
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4-monooxygenase
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propyne
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dinuclear
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rhodochrous
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smmos
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epoxygenation
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epoxyethane
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corallinus
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autotrophicus
- 1.14.13.69
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epoxidation
- xanthobacter
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vinyl
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diiron
- nocardioides
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4-monooxygenase
- propyne
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dinuclear
- rhodochrous
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smmos
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epoxygenation
- epoxyethane
- corallinus
- autotrophicus
Reaction
Synonyms
AkMO, alkene epoxygenase, alkene monooxygenase, AMO, ethene MO, EtnABCD, EtnC, etnD, IsoMO, isoprene monooxygenase, More, PmoABCD, propene MO, propene monooxygenase, XAMO
ECTree
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General Information
General Information on EC 1.14.13.69 - alkene monooxygenase
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evolution
additional information
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the endogenous IsoF component may be required to restore activity
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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
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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
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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
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