Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NDH-2 | type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview | Methylococcus capsulatus |
Crystallization (Comment) | Organism |
---|---|
enzyme pMMO crystal structure analysis, PDB ID 3RGB | Methylococcus capsulatus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | membrane-bound | Methylococcus capsulatus | 16020 | - |
membrane | membrane-bound | Methylocystis sp. M | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylococcus capsulatus | |
copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylosinus trichosporium | |
copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylocystis sp. | |
Cu2+ | required for activity, enzyme pMMO has a copper active site. dicopper site occupied with a two copper ions or b one copper ion from Methylocystis speciesstrain M, structure comparisons, modeling | Methylocystis sp. M | |
Cu2+ | required for activity, enzyme pMMO has a copper active site. Subdomain with a Cu-Cu distance of about 2.5 A, ligated by the N-terminal amino group and side chain of His33 (Cu1) as well as His137 and His139 (Cu2), and a zinc ion in PmoC about 20 A away from the PmoB dicopper site and attributed to the crystallization solution | Methylococcus capsulatus | |
Zn2+ | binds in the copper active site | Methylococcus capsulatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + quinol + O2 | Methylococcus capsulatus | - |
methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | Methylocystis sp. M | - |
methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | Methylococcus capsulatus Bath | - |
methanol + quinone + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylococcus capsulatus | - |
- |
- |
Methylococcus capsulatus | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
Methylococcus capsulatus Bath | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
Methylococcus capsulatus Bath. | - |
- |
- |
Methylocystis sp. | - |
- |
- |
Methylocystis sp. M | - |
- |
- |
Methylocystis sp. Rockwell | - |
- |
- |
Methylosinus trichosporium | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
methane + quinol + O2 = methanol + quinone + H2O | reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview | Methylococcus capsulatus | |
methane + quinol + O2 = methanol + quinone + H2O | reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview | Methylocystis sp. M |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + quinol + O2 | - |
Methylococcus capsulatus | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | - |
Methylocystis sp. M | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | - |
Methylococcus capsulatus Bath | methanol + quinone + H2O | - |
? | |
methane + reduced acceptor + H* + O2 | - |
Methylococcus capsulatus | methanol + acceptor + H2O | - |
? | |
methane + reduced acceptor + H* + O2 | - |
Methylococcus capsulatus Bath | methanol + acceptor + H2O | - |
? | |
methane + succinate + O2 | membrane-bound enzyme only | Methylococcus capsulatus | methanol + fumarate + H2O | - |
? | |
methane + succinate + O2 | membrane-bound enzyme only | Methylococcus capsulatus Bath | methanol + fumarate + H2O | - |
? | |
additional information | activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples | Methylococcus capsulatus | ? | - |
? | |
additional information | activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples | Methylococcus capsulatus Bath | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
pMMO | - |
Methylococcus capsulatus |
pMMO | - |
Methylosinus trichosporium |
pMMO | - |
Methylocystis sp. |
pMMO | - |
Methylocystis sp. M |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
quinol | - |
Methylococcus capsulatus | |
quinol | - |
Methylocystis sp. M |
General Information | Comment | Organism |
---|---|---|
evolution | methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available | Methylococcus capsulatus |
evolution | methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available | Methylocystis sp. M |
additional information | enzyme pMMO contains a copper active site, active site structure, overview | Methylocystis sp. M |
additional information | enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-Oยท) species | Methylococcus capsulatus |
physiological function | methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO) | Methylococcus capsulatus |
physiological function | methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO) | Methylocystis sp. M |