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Literature summary extracted from
- Why orfY? Characterization of MMOD, a long overlooked component of the soluble methane monooxygenase from Methylococcus capsulatus (Bath) (2002), J. Biol. Chem., 277, 5858-5865.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.13.25 | DNA sequence analysis | Methylococcus capsulatus |
| 1.14.13.25 | overexpression of an additional protein component D of sMMO encoded by orfY as thioredoxin-fusion protein with His-Tag in Escherichia coli, protein component D is termed MMOD | Methylococcus capsulatus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.14.13.25 | sMMO is more stable and easier to purify than pMMO | Methylococcus capsulatus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.25 | additional information | sMMO is completely inhibited by monomeric component D, but not by dimeric, monomeric MMOD is interfering with the catalytically active complex between component A hydroxylase and component protein B | Methylococcus capsulatus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.13.25 | cytoplasm | cytoplasmatic, soluble enzyme form termed sMMO | Methylococcus capsulatus | 5737 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.25 | 12000 | - |
component D of sMMO: 2 * 12000, SDS-PAGE | Methylococcus capsulatus |
| 1.14.13.25 | 24000 | - |
component D of sMMO, forms homodimers, gel filtration | Methylococcus capsulatus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.25 | Methylococcus capsulatus | - |
Bath | - |
| 1.14.13.25 | Methylococcus capsulatus Bath | - |
Bath | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.13.25 | component D of sMMO recombinant from Escherichia coli as His-tagged thioredoxin-fusion protein, the thioredoxin is cleaved off during purification by factor Xa | Methylococcus capsulatus |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.13.25 | methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | modeling of interaction between the different protein components of sMMO | Methylococcus capsulatus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.25 | methane + NAD(P)H + O2 | - |
Methylococcus capsulatus | methanol + NAD(P)+ + H2O | - |
? |  |
| 1.14.13.25 | methane + NAD(P)H + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD(P)+ + H2O | - |
? | |
| 1.14.13.25 | propylene + NAD(P)H + O2 | enzyme form sMMO | Methylococcus capsulatus | propylene oxide + NADP+ + H2O | - |
? | |
| 1.14.13.25 | propylene + NAD(P)H + O2 | enzyme form sMMO | Methylococcus capsulatus Bath | propylene oxide + NADP+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | ? | - |
Methylococcus capsulatus |
| 1.14.13.25 | dimer | component D of sMMO: 2 * 12000, SDS-PAGE | Methylococcus capsulatus |
| 1.14.13.25 | More | sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D | Methylococcus capsulatus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | MMO | - |
Methylococcus capsulatus |
| 1.14.13.25 | pMMO | particulate, membrane-bound enzyme form | Methylococcus capsulatus |
| 1.14.13.25 | sMMO | soluble, cytoplasmic enzyme form | Methylococcus capsulatus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.25 | 25 | - |
assay at | Methylococcus capsulatus |
| 1.14.13.25 | 25 | - |
enzyme form sMMO | Methylococcus capsulatus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.25 | additional information | - |
additional information | - |
Methylococcus capsulatus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.25 | 7 | - |
assay at | Methylococcus capsulatus |
| 1.14.13.25 | 7 | - |
enzyme form sMMO | Methylococcus capsulatus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.25 | FAD | protein C, reductase component: contains 1 mol FAD per mol protein | Methylococcus capsulatus | |
| 1.14.13.25 | additional information | component D contains no metal ions or organic cofactors | Methylococcus capsulatus | |
| 1.14.13.25 | NADH | - |
Methylococcus capsulatus | |
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