EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Fe2+ | activation of dioxygen occurs at a diiron centre within the hydroxylase subunit. The monooxygenation of a substrate by sMMO requires only two oxidation equivalents, and, consequently, after the oxygenation the two iron centres remain in the oxidation state +III | Bacteria |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.25 | Bacteria | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + O2 | consists of three subunits, the hydroxylase (MMOH), at which the oxidation of methane takes place, the reductase (MMOR) and a small regulating unit MMOB | Bacteria | methanol + NAD(P)+ + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.25 | sMMO | - |
Bacteria |
1.14.13.25 | soluble methane monooxygenase | - |
Bacteria |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | NADH | two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles | Bacteria | |
1.14.13.25 | NADPH | - |
Bacteria |