Application | Comment | Organism |
---|---|---|
synthesis | the enzyme is a base or scaffold for design of small molecule catalysts for use in large scale methanol synthesis | Methylophilaceae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutagenesis of MMOB potentially broadening the substrate range of the enzyme | Methylophilaceae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the enzyme contains a Fe2S2 cluster, a bis-my-hydroxo-bridged dinuclear iron cluster, that binds to the enzyme reductase domain MMOR | Methylophilaceae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NADH + O2 | Methylophilaceae | methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 | methanol + NAD+ + H2O | - |
? | |
additional information | Methylophilaceae | access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylophilaceae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | reaction mechanism and regulation, catalytic cycle of sMMO, the enzyme complex causes quantum tunneling to dominate in CĀH bond cleavage reaction for methane, selectively increasing the rate for this substrate, mechanism of C-H bond cleavage, overview | Methylophilaceae |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:methane-grown cell | - |
Methylophilaceae | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NADH + O2 | methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 | Methylophilaceae | methanol + NAD+ + H2O | - |
? | |
methane + NADH + O2 | for the MMOH alone the rate of turnover is increased 150fold and rate constant for O2 binding is increased 1000fold in the binary complex compared to the complete enzyme | Methylophilaceae | methanol + NAD+ + H2O | - |
? | |
additional information | access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview | Methylophilaceae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in CĀH bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview | Methylophilaceae |
Synonyms | Comment | Organism |
---|---|---|
sMMO | - |
Methylophilaceae |
soluble methane monooxygenase | - |
Methylophilaceae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | binds to the enzyme reductase protein MMOR | Methylophilaceae | |
NADH | binds to the enzyme hydroxylase protein MMOH | Methylophilaceae |