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Literature summary for 1.14.13.25 extracted from
- Low-molecular-weight analogues of the soluble methane monooxygenase (sMMO): from the structural mimicking of resting states and intermediates to functional models (2009), Chemistry, 15, 10316-10328.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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 |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacteria | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| sMMO | - |
Bacteria |
| soluble methane monooxygenase | - |
Bacteria |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles | Bacteria | |
| NADPH | - |
Bacteria | |
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