EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
   1.14.13.25 | more |
a colorimetric assay is adopted for the sMMO activity detection of biofilm |
Methylosinus trichosporium |
? |
- |
- |
| 1.14.13.25 | more |
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds |
Methylosinus sporium |
? |
- |
- |
| 1.14.13.25 | more |
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane |
Methylosinus sporium |
? |
- |
- |
| 1.14.13.25 | more |
the soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions |
Methylomonas methanica |
? |
- |
- |
| 1.14.13.25 | more |
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds |
Methylosinus sporium 5 |
? |
- |
- |
| 1.14.13.25 | more |
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane |
Methylosinus sporium 5 |
? |
- |
- |
| 1.14.13.25 | more |
the soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions |
Methylomonas methanica MC09 |
? |
- |
- |
| 1.14.13.25 | more |
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds |
Methylosinus sporium ATCC 35069 |
? |
- |
- |
| 1.14.13.25 | more |
sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane |
Methylosinus sporium ATCC 35069 |
? |
- |
- |
| 1.14.13.25 | 1,1,2,2-tetramethylcyclopropane + NADH + O2 |
- |
Methylosinus trichosporium |
? |
- |
? |
