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
ECTree
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Activating Compound
Activating Compound on EC 1.14.18.3 - methane monooxygenase (particulate)
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bacteriohemerythrin
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enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1
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catalase
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increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity
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lauryl maltoside
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the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization
methanobactin-Cu2+ complex
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stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b
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NDH-2
type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview
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pMMO with the full complement of copper ions does not require methanobactin for activity
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additional information
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the active center of pMH is located in the beta-subunit
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additional information
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no pMMO acivity is observed in the detergent-solubilized fraction in the presence of dithionite, ascorbate, or methyl viologen. No pMMO activity with duroquinol or NADH is observed after solubilization with Triton X-100, Tween 20, zwittergent 3-12, Nonidet-P40, or synperonic
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