EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.13.25 | T111Y | the T111Y variant of MMOB causes only a small increase in reactivity | Methylosinus trichosporium |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Fe2+ | contains Fe2+ | Methylosinus trichosporium |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.25 | Methylosinus trichosporium | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | catalyzes the oxidation of methane through the activation of O2 at a nonheme biferrous center in the hydroxylase component MMOH | Methylosinus trichosporium |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + H+ + O2 | - |
Methylosinus trichosporium | methanol + NAD(P)+ + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.25 | MMOB | cofactor-free, monomeric component of sMMO, has regulatory role in catalysis | Methylosinus trichosporium |
1.14.13.25 | MMOH | hydroxylase component of sMMO, contains a binuclear nonheme iron active site that is essential for O2 activation and subsequent methane oxidation | Methylosinus trichosporium |
1.14.13.25 | MMOR | reductase component of sMMO, contains a FAD cofactor and a [2Fe-2S] cluster, is responsible for transferring the reducing equivalents from NAD(P)H to MMOH | Methylosinus trichosporium |
1.14.13.25 | sMMO | - |
Methylosinus trichosporium |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | FAD | - |
Methylosinus trichosporium | |
1.14.13.25 | NADH | - |
Methylosinus trichosporium | |
1.14.13.25 | NADPH | - |
Methylosinus trichosporium |