EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.18.3 | recombinant expression of wild-type holoenzyme and truncated recombinant periplasmic domains of pMMO (spmoB) | Methylococcus capsulatus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.18.3 | membrane | membrane-bound | Methylococcus capsulatus | 16020 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.18.3 | 300000 | - |
alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits | Methylococcus capsulatus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.18.3 | methane + quinol + O2 | Methylococcus capsulatus | - |
methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | Methylococcus capsulatus Bath | - |
methanol + quinone + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.18.3 | Methylococcus capsulatus | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
1.14.18.3 | Methylococcus capsulatus Bath | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.18.3 | native holoenzyme from isolated membranes by solubilization with detergent n-dodecyl beta-D-maltoside, ultrafiltration, and gel filtration | Methylococcus capsulatus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.18.3 | methane + quinol + O2 | - |
Methylococcus capsulatus | methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | - |
Methylococcus capsulatus Bath | methanol + quinone + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.18.3 | 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 | Methylococcus capsulatus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.18.3 | particulate MMO | - |
Methylococcus capsulatus |
1.14.18.3 | pMMO | - |
Methylococcus capsulatus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.3 | additional information | the pMMO electron donor is generally thought to be ubiquinol generated by a type 2 NADH:quinone oxidoreductase. The addition of cytochrome could facilitate electron transfer without the requirement for NADH | Methylococcus capsulatus | |
1.14.18.3 | quinol | the cofactor receives electrons from NADH | Methylococcus capsulatus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.18.3 | metabolism | in the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Membrane-bound particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex, interaction analysis and biolayer interferometry studies demonstrate specific protein-protein interactions between methanol dehydrogenase (MDH) and Methyylococcus capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of pMMO (spmoB), kinetics, overview | Methylococcus capsulatus |