Application | Comment | Organism |
---|---|---|
energy production | teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) | Methylococcus capsulatus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Methylosinus trichosporium | 16020 | - |
membrane | - |
Methylocystis sp. | 16020 | - |
membrane | membrane-bound | Methylococcus capsulatus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylosinus trichosporium | |
copper | the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. | |
Cu2+ | required for activity, each of pmoA, pmoB, and pmoC houses a dicopper center | Methylococcus capsulatus | |
additional information | the pMMO active site might possess a di-iron center located at the transmembrane zinc/copper site | Methylococcus capsulatus | |
Zn2+ | enzyme-bound | 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 | Methylococcus capsulatus Bath | - |
methanol + quinone + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylococcus capsulatus | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
Methylococcus capsulatus Bath | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
Methylocystis sp. | - |
- |
- |
Methylocystis sp. Rockwell | - |
- |
- |
Methylosinus trichosporium | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + quinol + O2 | - |
Methylococcus capsulatus | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylosinus trichosporium | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | - |
Methylococcus capsulatus Bath | methanol + quinone + H2O | - |
? | |
methane + quinol + O2 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. Rockwell | methanol + quinone + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotrimer | enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites | Methylococcus capsulatus |
Synonyms | Comment | Organism |
---|---|---|
particulate methane monooxygenase | - |
Methylosinus trichosporium |
particulate methane monooxygenase | - |
Methylocystis sp. |
particulate methane monooxygenase | - |
Methylococcus capsulatus |
pMMO | - |
Methylosinus trichosporium |
pMMO | - |
Methylocystis sp. |
pMMO | - |
Methylococcus capsulatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Methylococcus capsulatus |
40 | 45 | - |
Methylosinus trichosporium |
40 | 45 | - |
Methylocystis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | 7.3 | - |
Methylosinus trichosporium |
7.2 | 7.3 | - |
Methylocystis sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | methane activation by particulate methane monooxygenase is NAD-dependent | Methylosinus trichosporium | |
NAD+ | methane activation by particulate methane monooxygenase is NAD-dependent. Docking simulations of NAD+ on the enzyme clearly show preferential binding of the cofactor in the vicinity of the Cu metal centers confirming its functional relationship with particulate methane monooxygenase | Methylocystis sp. | |
quinol | - |
Methylococcus capsulatus |
General Information | Comment | Organism |
---|---|---|
additional information | analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview | Methylococcus capsulatus |
physiological function | MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol | Methylococcus capsulatus |