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Literature summary extracted from

  • Murrell, J.C.; Gilbert, B.; McDonald, I.R.
    Molecular biology and regulation of methane monooxygenase (2000), Arch. Microbiol., 173, 325-332.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.25 expressed in Escherichia coli Methylococcus capsulatus
1.14.13.25 expressed in Escherichia coli Methylomicrobium album
1.14.13.25 expressed in Escherichia coli Methylocystis sp.
1.14.18.3 expressed in Escherichia coli Methylococcus capsulatus
1.14.18.3 expressed in Escherichia coli Methylomicrobium album
1.14.18.3 expressed in Escherichia coli Methylocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.25 Cu2+ copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component Methylococcus capsulatus
1.14.13.25 Cu2+ copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component Methylocystis sp.
1.14.13.25 Cu2+ copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component Methylomicrobium album

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.25 cytoplasm
-
 Methylococcus capsulatus 5737
-
1.14.13.25 cytoplasm
-
 Methylomicrobium album 5737
-
1.14.13.25 cytoplasm
-
 Methylocystis sp. 5737
-
1.14.18.3 membrane
-
 Methylococcus capsulatus 16020
-
1.14.18.3 membrane
-
 Methylomicrobium album 16020
-
1.14.18.3 membrane
-
 Methylocystis sp. 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.3 Cu2+ the active enzyme contains approximately 15 copper atoms per mol Methylococcus capsulatus
1.14.18.3 Cu2+ the active enzyme contains approximately 15 copper atoms per mol Methylocystis sp.
1.14.18.3 Cu2+ the active enzyme contains approximately 15 copper atoms per mol enzyme Methylomicrobium album
1.14.18.3 Fe2+ the active enzyme contains 2 iron atoms per mol Methylococcus capsulatus
1.14.18.3 Fe2+ the active enzyme contains 2 iron atoms per mol Methylocystis sp.
1.14.18.3 Fe2+ the active enzyme contains 2 iron atoms per mol enzyme Methylomicrobium album

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.18.3 23000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylococcus capsulatus
1.14.18.3 23000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylomicrobium album
1.14.18.3 23000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylocystis sp.
1.14.18.3 27000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylococcus capsulatus
1.14.18.3 27000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylomicrobium album
1.14.18.3 27000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylocystis sp.
1.14.18.3 45000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylococcus capsulatus
1.14.18.3 45000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylomicrobium album
1.14.18.3 45000
-
 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.25 methane + duroquinol + O2 Methylococcus capsulatus
-
 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2 Methylomicrobium album
-
 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2 Methylocystis sp.
-
 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2 Methylococcus capsulatus Bath
-
 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2 Methylomicrobium album BG8
-
 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2 Methylococcus capsulatus
-
 methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2 Methylomicrobium album
-
 methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2 Methylocystis sp.
-
 methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2 Methylococcus capsulatus Bath
-
 methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2 Methylomicrobium album BG8
-
 methanol + acceptor + H2O
-
 ?
1.14.13.25 additional information Methylococcus capsulatus the sMMO enzyme has broad substrate specificity compared to pMMO ?
-
 ?
1.14.13.25 additional information Methylomicrobium album the sMMO enzyme has broad substrate specificity compared to pMMO ?
-
 ?
1.14.13.25 additional information Methylocystis sp. the sMMO enzyme has broad substrate specificity compared to pMMO ?
-
 ?
1.14.13.25 additional information Methylococcus capsulatus Bath the sMMO enzyme has broad substrate specificity compared to pMMO ?
-
 ?
1.14.13.25 additional information Methylomicrobium album BG8 the sMMO enzyme has broad substrate specificity compared to pMMO ?
-
 ?
1.14.18.3 methane + duroquinol + O2 Methylococcus capsulatus
-
 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2 Methylomicrobium album
-
 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2 Methylocystis sp.
-
 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2 Methylococcus capsulatus Bath
-
 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2 Methylomicrobium album BG8
-
 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2 Methylococcus capsulatus
-
 methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2 Methylomicrobium album
-
 methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2 Methylocystis sp.
-
 methanol + acceptor + H2O
-
 ?
1.14.18.3 additional information Methylococcus capsulatus unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds ?
-
 ?
1.14.18.3 additional information Methylomicrobium album unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds ?
-
 ?
1.14.18.3 additional information Methylocystis sp. unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds ?
-
 ?
1.14.18.3 additional information Methylococcus capsulatus Bath unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds ?
-
 ?
1.14.18.3 additional information Methylomicrobium album BG8 unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus
-
-
-
1.14.13.25 Methylococcus capsulatus Bath
-
-
-
1.14.13.25 Methylocystis sp.
-
-
-
1.14.13.25 Methylomicrobium album
-
-
-
1.14.13.25 Methylomicrobium album BG8
-
-
-
1.14.18.3 Methylococcus capsulatus
-
-
-
1.14.18.3 Methylococcus capsulatus Bath
-
-
-
1.14.18.3 Methylocystis sp.
-
-
-
1.14.18.3 Methylomicrobium album
-
-
-
1.14.18.3 Methylomicrobium album BG8
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + duroquinol + O2
-
 Methylococcus capsulatus methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2
-
 Methylomicrobium album methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2
-
 Methylocystis sp. methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2
-
 Methylococcus capsulatus Bath methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + duroquinol + O2
-
 Methylomicrobium album BG8 methanol + duroquinone + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2
-
 Methylomicrobium album methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2
-
 Methylocystis sp. methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus Bath methanol + acceptor + H2O
-
 ?
1.14.13.25 methane + reduced acceptor + H* + O2
-
 Methylomicrobium album BG8 methanol + acceptor + H2O
-
 ?
1.14.13.25 additional information the sMMO enzyme has broad substrate specificity compared to pMMO Methylococcus capsulatus ?
-
 ?
1.14.13.25 additional information the sMMO enzyme has broad substrate specificity compared to pMMO Methylomicrobium album ?
-
 ?
1.14.13.25 additional information the sMMO enzyme has broad substrate specificity compared to pMMO Methylocystis sp. ?
-
 ?
1.14.13.25 additional information the sMMO enzyme has broad substrate specificity compared to pMMO Methylococcus capsulatus Bath ?
-
 ?
1.14.13.25 additional information the sMMO enzyme has broad substrate specificity compared to pMMO Methylomicrobium album BG8 ?
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylococcus capsulatus methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylomicrobium album methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylocystis sp. methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylococcus capsulatus Bath methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylomicrobium album BG8 methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2
-
 Methylococcus capsulatus methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2
-
 Methylomicrobium album methanol + acceptor + H2O
-
 ?
1.14.18.3 methane + reduced acceptor + H* + O2
-
 Methylocystis sp. methanol + acceptor + H2O
-
 ?
1.14.18.3 additional information unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds Methylococcus capsulatus ?
-
 ?
1.14.18.3 additional information unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds Methylomicrobium album ?
-
 ?
1.14.18.3 additional information unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds Methylocystis sp. ?
-
 ?
1.14.18.3 additional information unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds Methylococcus capsulatus Bath ?
-
 ?
1.14.18.3 additional information unlike the sMMO, the pMMO enzyme has relatively narrow substrate specificity, oxidising alkanes and alkenes of up to five carbons but not aromatic compounds Methylomicrobium album BG8 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.18.3 heterotrimer 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylococcus capsulatus
1.14.18.3 heterotrimer 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylomicrobium album
1.14.18.3 heterotrimer 1 * 45000 + 1 * 27000 + 1 * 23000, SDS-PAGE Methylocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 sMMO
-
 Methylococcus capsulatus
1.14.13.25 sMMO
-
 Methylomicrobium album
1.14.13.25 sMMO
-
 Methylocystis sp.
1.14.13.25 soluble methane monooxygenase
-
 Methylococcus capsulatus
1.14.13.25 soluble methane monooxygenase
-
 Methylomicrobium album
1.14.13.25 soluble methane monooxygenase
-
 Methylocystis sp.
1.14.18.3 particulate methane monooxygenase
-
 Methylococcus capsulatus
1.14.18.3 particulate methane monooxygenase
-
 Methylomicrobium album
1.14.18.3 particulate methane monooxygenase
-
 Methylocystis sp.
1.14.18.3 pMMO
-
 Methylococcus capsulatus
1.14.18.3 pMMO
-
 Methylomicrobium album
1.14.18.3 pMMO
-
 Methylocystis sp.

Expression

EC Number Organism Comment Expression
1.14.13.25 Methylococcus capsulatus transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4 down
1.14.13.25 Methylomicrobium album transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4 down
1.14.13.25 Methylocystis sp. transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4 down
1.14.13.25 Methylococcus capsulatus the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+) up
1.14.13.25 Methylomicrobium album the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+) up
1.14.13.25 Methylocystis sp. the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+) up
1.14.18.3 Methylococcus capsulatus the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios up
1.14.18.3 Methylomicrobium album the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios up
1.14.18.3 Methylocystis sp. the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios up