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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results (Cofactor
Cofactor on EC 1.14.13.69 - alkene monooxygenase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ferredoxin
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only contains a Rieske-type [2Fe-2S] cluster, characterization of the Rieske protein component (IsoC) of isoprene monooxygenase from Rhodococcus sp. AD45, 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
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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additional information
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the reductase component contains two cofactors, an FAD and a [2Fe-2S] cluster, whereas the ferredoxin only contains a Rieske-type [2Fe-2S] cluster. These redox active components are involved in the transfer of electrons, from NADH via the reductase, and the Rieske protein in four-component SDIMOs, to the diiron active site of the oxygenase
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