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. |
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 |
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 | - |
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 |
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. |
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 | ? | - |
? |
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 | - |
- |
- |
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 | ? | - |
? |
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. |
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. |
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 |