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Literature summary for 1.14.13.25 extracted from
- Biocatalytic oxidations of substrates through soluble methane monooxygenase from Methylosinus sporium 5 (2018), Catalysts, 8, 582 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| quantitative expression analysis of subunits alpha, beta and gamma | Methylosinus sporium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5 | Methylosinus sporium |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | - |
Methylosinus sporium |  |
| additional information | other possible inhibitory enzymes, such as MMOD (orfY), can inhibit its activity in the soluble portion of cell lysates | Methylosinus sporium | |
| Ni2+ | - |
Methylosinus sporium | |
| Zn2+ | - |
Methylosinus sporium | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | the presence of iron at the diiron active site is required for the catalytic activity of the sMMO | Methylosinus sporium | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methane + NADH + H+ + O2 | Methylosinus sporium | - |
methanol + NAD+ + H2O | - |
? | |
| methane + NADH + H+ + O2 | Methylosinus sporium 5 | - |
methanol + NAD+ + H2O | - |
? | |
| methane + NADH + H+ + O2 | Methylosinus sporium ATCC 35069 | - |
methanol + NAD+ + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylosinus sporium | - |
- |
- |
| Methylosinus sporium 5 | - |
- |
- |
| Methylosinus sporium ATCC 35069 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant subunits from Escherichia coli strain BL21(DE3) by two different steps of anion exchange chromatography, and gel filtration | Methylosinus sporium |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell culture | cultured in copper-limited NMS media | Methylosinus sporium | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 494 | - |
purified recombinant catalytic subunit MMOH, pH 7.5, 30°C | Methylosinus sporium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzene + NADH + H+ + O2 | - |
Methylosinus sporium | ? | - |
? | |
| benzene + NADH + H+ + O2 | - |
Methylosinus sporium 5 | ? | - |
? | |
| benzene + NADH + H+ + O2 | - |
Methylosinus sporium ATCC 35069 | ? | - |
? | |
| dichloroethane + NADH + O2 | - |
Methylosinus sporium | ethanol + 2 Cl- + NAD+ + H2O | - |
? | |
| dichloroethane + NADH + O2 | - |
Methylosinus sporium 5 | ethanol + 2 Cl- + NAD+ + H2O | - |
? | |
| dichloroethane + NADH + O2 | - |
Methylosinus sporium ATCC 35069 | ethanol + 2 Cl- + NAD+ + H2O | - |
? | |
| dichloropropane + NADH + O2 | - |
Methylosinus sporium | propanol + 2 Cl- + NAD+ + H2O | - |
? | |
| heptane + NADH + O2 | - |
Methylosinus sporium | 1-heptanol + 2-heptanol + NAD+ + H2O | - |
? | |
| methane + NADH + H+ + O2 | - |
Methylosinus sporium | methanol + NAD+ + H2O | - |
? | |
| methane + NADH + H+ + O2 | - |
Methylosinus sporium 5 | methanol + NAD+ + H2O | - |
? | |
| methane + NADH + H+ + O2 | - |
Methylosinus sporium ATCC 35069 | methanol + NAD+ + H2O | - |
? | |
| additional information | enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds | Methylosinus sporium | ? | - |
- |
|
| additional information | enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds | Methylosinus sporium 5 | ? | - |
- |
|
| additional information | enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds | Methylosinus sporium ATCC 35069 | ? | - |
- |
|
| toluene + NADH + H+ + O2 | - |
Methylosinus sporium | ? | - |
? | |
| toluene + NADH + H+ + O2 | - |
Methylosinus sporium 5 | ? | - |
? | |
| toluene + NADH + H+ + O2 | - |
Methylosinus sporium ATCC 35069 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | (alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE | Methylosinus sporium |
| More | the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR) | Methylosinus sporium |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| sMMO | - |
Methylosinus sporium |
| soluble methane monooxygenase | - |
Methylosinus sporium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Methylosinus sporium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Methylosinus sporium |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the FAD-containing domain MMOR-FAD consits of MMOR residues 97-343 | Methylosinus sporium | |
| NADH | NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands | Methylosinus sporium | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme sMMO belongs to the BMM superfamily | Methylosinus sporium |
| additional information | interaction analysis of sMMO subunits and structure-function analysis, detailed overview. Alterations of hydrogen bonding or solvent accessibility occur due to the conformational changes of isoalloxazine in FAD | Methylosinus sporium |
| physiological function | in the enzyme complex of sMMO, Two molar equivalents of MMOB are necessary to achieve catalytic activities and oxidized a broad range of substrates including alkanes, alkenes, halogens, and aromatics. Optimal activities are observed at pH 7.5 for most substrates possibly because of the electron transfer environment in MMOR. The presence of iron at the diiron active site is required for the catalytic activity of the sMMO. Secretion of siderophores could be a defense mechanism of Methylosinus sporium strain 5 in growth condition of high bacterial concentrations and limited iron concentration. A possible explanation is that Methylosinus sporium strain 5 responds more sensitively than other type II methanotrophs because this methanotroph generates a brown-black pigment in response to a high cell:iron ratio. MMOR is an essential component for the catalytic cycle owing to its electron transfer abilities, which are accomplished by FAD-containing and [2Fe-2S] cluster ferredoxin domains to reduce diiron active sites in MMOH. NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands | Methylosinus sporium |
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