1.14.13.25: methane monooxygenase (soluble)
This is an abbreviated version!
For detailed information about methane monooxygenase (soluble), go to the full flat file.
Word Map on EC 1.14.13.25
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1.14.13.25
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methanotrophs
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methanol
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methylosinus
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capsulatus
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methylococcus
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trichosporium
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methane-oxidizing
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methylocystis
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ch4
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methylomonas
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dioxygen
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dinuclear
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methylobacter
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trichloroethylene
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methylomicrobium
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alkane
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diironii
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ammonia-oxidizing
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landfill
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upland
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antiferromagnetically
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wetland
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high-valent
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non-motile
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copper-containing
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carboxylate-bridged
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peat
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copper-dependent
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dicopper
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ch3oh
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nitrosomonas
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cometabolic
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diferrous
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methanobactins
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energy production
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mixed-valent
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gammaproteobacterial
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sphagnum
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t-rflp
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seep
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propene
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synthesis
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biotechnology
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degradation
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exafs
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nitrify
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peroxo
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
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methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
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dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
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diironii
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ammonia-oxidizing
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landfill
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upland
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antiferromagnetically
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wetland
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high-valent
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non-motile
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copper-containing
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carboxylate-bridged
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peat
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copper-dependent
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dicopper
- ch3oh
- nitrosomonas
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cometabolic
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diferrous
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methanobactins
- energy production
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mixed-valent
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gammaproteobacterial
- sphagnum
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t-rflp
-
seep
- propene
- synthesis
- biotechnology
- degradation
-
exafs
-
nitrify
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peroxo
Reaction
Synonyms
chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase
ECTree
1.14.13.25 methane monooxygenase (soluble)Advanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.14.13.25 - methane monooxygenase (soluble)
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NATURAL SUBSTRATE 
NATURAL 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
methane + duroquinol + O2
methanol + duroquinone + H2O
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?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
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?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
Methylococcus capsulatus Bath.
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
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?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
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?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
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?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
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initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
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?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
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initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
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?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
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?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
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?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
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?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
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?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
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-
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?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
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?
methane + NADH + O2
methanol + NAD+ + H2O
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?
methane + NADH + O2
methanol + NAD+ + H2O
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via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
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?
methane + NADH + O2
methanol + NAD+ + H2O
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via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
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?
methane + NADH + O2
methanol + NAD+ + H2O
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?
methane + NADH + O2
methanol + NAD+ + H2O
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methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2
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?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
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?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
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?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
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?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
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?
additional information
?
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the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
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?
additional information
?
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the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
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?
additional information
?
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the sMMO enzyme has broad substrate specificity compared to pMMO
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?
additional information
?
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the sMMO enzyme has broad substrate specificity compared to pMMO
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?
additional information
?
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the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
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-
?
additional information
?
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the sMMO enzyme has broad substrate specificity compared to pMMO
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?
additional information
?
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the sMMO enzyme has broad substrate specificity compared to pMMO
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?
additional information
?
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the sMMO enzyme has broad substrate specificity compared to pMMO
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?
additional information
?
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access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview
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?
