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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Subunits
Subunits on EC 1.14.18.3 - methane monooxygenase (particulate)
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heterotrimer
hexamer
oligomer
trimer
additional information
heterotrimer
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1 * 42785 + 1 * 29733 + 1 * 28328, MALDI-TOF mass spectrometry
heterotrimer
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1 * 47000 + 1 * 24000 + 1 * 22000, X-ray crystallography
heterotrimer
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pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
heterotrimer
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1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
heterotrimer
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1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
heterotrimer
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1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE
heterotrimer
alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits
heterotrimer
enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites
heterotrimer
the enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an alpha3beta3gamma3 trimer
heterotrimer
the pMMO is an about 300 kDa alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits. The pmoA and pmoC subunits are composed primarily of transmembrane helices, and pmoB consists of two periplasmic cupredoxin-like domains linked by two transmembrane helices. The active site is proposed to be a dinuclear copper center located in the N-terminal pmoB periplasmic domain close to the membrane interface
heterotrimer
three pMMO subunits confirmed by mass spectrometry
heterotrimer
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1 * 42785 + 1 * 29073 + 1 * 28328, MALDI-TOF mass spectrometry
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heterotrimer
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1 * 42786 + 1 * 29063 + 1 * 28376, calculated from amino acid sequence
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heterotrimer
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the pMMO is an about 300 kDa alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits. The pmoA and pmoC subunits are composed primarily of transmembrane helices, and pmoB consists of two periplasmic cupredoxin-like domains linked by two transmembrane helices. The active site is proposed to be a dinuclear copper center located in the N-terminal pmoB periplasmic domain close to the membrane interface
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heterotrimer
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the enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an alpha3beta3gamma3 trimer
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heterotrimer
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alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits
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heterotrimer
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enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites
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heterotrimer
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pMH, 1 * 47000, + 1 * 27000 + 1 * 25000, alphabetagamma-subunit, SDS-PAGE
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trimer
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1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
trimer
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1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
trimer
1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE
trimer
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1 * 47000 + 1 * 26000 + 1 * 23000, three-dimensional structure analysis of purified pMMO by electron microscopy and single-particle analysis at 23 A resolution, overview
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trimer
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1 * 47000 + 1 * 27000 + 1 * 25000, pMMO, mass spectrometry and SDS-PAGE
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trimer
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1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE
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pMMO subunit A has acetylene binding ability
additional information
enzyme structure comparisons, overview
additional information
enzyme pMMO is a large protein complex with three subunits, PmoA, PmoB and PmoC, and many copper ions, three-dimensional structure of pMMO, overview
additional information
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pMMO subunit A has acetylene binding ability
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additional information
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enzyme pMMO is a large protein complex with three subunits, PmoA, PmoB and PmoC, and many copper ions, three-dimensional structure of pMMO, overview
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additional information
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three-dimensional structure determination and analysis
additional information
Methylocystis sp. Rockwell
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three-dimensional structure determination and analysis
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