1.14.18.3: methane monooxygenase (particulate)
This is an abbreviated version!
For detailed information about methane monooxygenase (particulate), go to the full flat file.
Word Map on EC 1.14.18.3
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1.14.18.3
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pmmos
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methanotrophs
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methylococcus
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capsulatus
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bath
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methylocystis
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methylosinus
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ch4
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trichosporium
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pmocab
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methylomicrobium
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duroquinol
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environmental protection
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analysis
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trinuclear
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nadh:quinone
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monocopper
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diiron
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ammonia-oxidizing
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energy production
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degradation
- 1.14.18.3
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pmmos
- methanotrophs
- methylococcus
- capsulatus
- bath
- methylocystis
- methylosinus
- ch4
- trichosporium
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pmocab
- methylomicrobium
- duroquinol
- environmental protection
- analysis
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trinuclear
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nadh:quinone
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monocopper
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diiron
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ammonia-oxidizing
- energy production
- degradation
Reaction
Synonyms
copper-containing membrane monooxygenase, copper-containing membrane-bound monooxygenase, CuMMO, membrane-associated methane monooxygenase, membrane-bound methane monooxygenase, membrane-embedded methane monooxygenase, methane hydroxylase, mMMO, MMO, particulate methane mono-oxygenase, particulate methane monooxygenas, particulate methane monooxygenase, particulate methane monooxygenase A, particulate methane-oxidizing complex, particulate MMO, PMH, pMMO, pMMO hydroxylase, pMMO-H, pMMO1, pMMO2, PmoA, PmoB, sMMO, soluble methane monooxygenase, spmoB
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Natural Substrates Products
Natural Substrates Products on EC 1.14.18.3 - methane monooxygenase (particulate)
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REACTION DIAGRAM
methane + duroquinol + O2
methanol + duroquinone + H2O
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methanol + quinone + H2O
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methane + quinol + O2
methanol + quinone + H2O
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methane + quinol + O2
methanol + quinone + H2O
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methane + quinol + O2
methanol + quinone + H2O
Methylococcus capsulatus (Bath) is a methanotroph that possesses both a membrane-embedded (pMMO) and a soluble methane monooxygenase (sMMO). Major changes takes place in the respiratory chain between pMMO- and sMMO-producing cells. Quinones are predominantly used as the electron donors for methane oxidation by pMMO. During production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
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methane + quinol + O2
methanol + quinone + H2O
Methylococcus capsulatus (Bath) is a methanotroph that possesses both a membrane-embedded (pMMO) and a soluble methane monooxygenase (sMMO). Major changes takes place in the respiratory chain between pMMO- and sMMO-producing cells. Quinones are predominantly used as the electron donors for methane oxidation by pMMO. During production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
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methane + quinol + O2
methanol + quinone + H2O
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methane + quinol + O2
methanol + quinone + H2O
Methylococcus capsulatus Bath.
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Methylococcus capsulatus (Bath) is a methanotroph that possesses both a membrane-embedded (pMMO) and a soluble methane monooxygenase (sMMO). Major changes takes place in the respiratory chain between pMMO- and sMMO-producing cells. Quinones are predominantly used as the electron donors for methane oxidation by pMMO. During production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation
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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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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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unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
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additional information
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unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
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?
additional information
?
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unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
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-
?
additional information
?
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-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
-
-
?
additional information
?
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-
unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds
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-
?