EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.13.25 | expression in Escherichia coli, determination of complete sMMO DNA gene sequence, phylogenetic analysis | Methylocystis sp. |
EC Number | General Stability | Organism |
---|---|---|
1.14.13.25 | Fe2+ stabilizes component C of sMMO | Methylocystis sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Co2+ | slightly, sMMO | Methylocystis sp. | |
1.14.13.25 | Cu2+ | causes protein aggregation | Methylocystis sp. | |
1.14.13.25 | Hg2+ | complete inhibition at 0.01 mM | Methylocystis sp. | |
1.14.13.25 | Ni2+ | causes protein aggregation; sMMO | Methylocystis sp. | |
1.14.13.25 | Zn2+ | causes protein aggregation; sMMO | Methylocystis sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.25 | 0.0064 | - |
NADH | sMMO component C reductase | Methylocystis sp. | |
1.14.13.25 | 5.2 | - |
NADPH | sMMO component C reductase | Methylocystis sp. |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.13.25 | cytoplasm | enzyme from cells grown under conditions of low copper availability | Methylocystis sp. | 5737 | - |
1.14.13.25 | cytoplasm | cytoplasmatic, soluble enzyme form termed sMMO | Methylocystis sp. | 5737 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Iron | 3.6 mol of iron per mol of hydroxylase component A | Methylocystis sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | additional information | - |
sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase | Methylocystis sp. |
1.14.13.25 | 18000 | - |
component protein B of sMMO | Methylocystis sp. |
1.14.13.25 | 23000 | - |
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE | Methylocystis sp. |
1.14.13.25 | 41000 | - |
component C reductase of sMMO | Methylocystis sp. |
1.14.13.25 | 43000 | - |
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE | Methylocystis sp. |
1.14.13.25 | 57000 | - |
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE | Methylocystis sp. |
1.14.13.25 | 229000 | - |
component A hydroxylase of sMMO | Methylocystis sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.25 | Methylocystis sp. | - |
- |
- |
1.14.13.25 | Methylocystis sp. | - |
enzyme form sMMO | - |
1.14.13.25 | Methylocystis sp. | - |
methanotroph type II | - |
1.14.13.25 | Methylocystis sp. WI 14 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.13.25 | sMMO with all components | Methylocystis sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | additional information | - |
component protein B is involved in enzyme regulation and enhances the activity 10fold | Methylocystis sp. |
1.14.13.25 | 0.0008 | - |
sMMO, substrate chloronaphthalene | Methylocystis sp. |
1.14.13.25 | 0.0012 | - |
sMMO, substrate naphthalene | Methylocystis sp. |
1.14.13.25 | 0.0039 | - |
sMMO, substrate chloropentane | Methylocystis sp. |
1.14.13.25 | 0.0122 | - |
sMMO, low copper growth concentration, growth substrate nitrate | Methylocystis sp. |
1.14.13.25 | 0.0191 | - |
sMMO, substrate butylene | Methylocystis sp. |
1.14.13.25 | 0.0254 | - |
sMMO, substrate propylene | Methylocystis sp. |
1.14.13.25 | 0.0336 | - |
sMMO, substrate ethylene | Methylocystis sp. |
1.14.13.25 | 0.205 | - |
sMMO, substrate diethylic ether | Methylocystis sp. |
1.14.13.25 | 0.334 | - |
sMMO, substrate propane | Methylocystis sp. |
EC Number | Storage Stability | Organism |
---|---|---|
1.14.13.25 | 4°C, sMMO component C reductase, 90% loss of activity after 120 h, can be restored by Fe2+ | Methylocystis sp. |
1.14.13.25 | sMMO component A hydroxylase is very unstable, splits into inactive subunits when stored frozen even for short periods | Methylocystis sp. |
1.14.13.25 | sMMO component protein B is stable when stored frozen | Methylocystis sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | benzene + NAD(P)H + H+ + O2 | - |
Methylocystis sp. | phenol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | bromobenzene + NAD(P)H + O2 | sMMO | Methylocystis sp. | bromophenol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | butane + NAD(P)H + O2 | - |
Methylocystis sp. | 1-butanol + 2-butanol + NAD(P)+ + H2O | only 2-butanol, sMMO | ? | |
1.14.13.25 | butylene + NAD(P)H + O2 | sMMO | Methylocystis sp. | butylene oxide + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | chlorobenzene + NAD(P)H + O2 | sMMO | Methylocystis sp. | chlorophenol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | chloronaphthalene + NAD(P)H + O2 | sMMO | Methylocystis sp. | chloronaphthol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | chloropentane + NAD(P)H + O2 | sMMO | Methylocystis sp. | chloropentanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | cyclohexane + NAD(P)H + O2 | sMMO | Methylocystis sp. | cyclohexanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | cytochrome c + NAD(P)H + O2 | sMMO | Methylocystis sp. | reduced cytochrome c + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | diethyl ether + NAD(P)H + O2 | sMMO | Methylocystis sp. | ethanol + ethanal + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | diethyl ether + NAD(P)H + O2 | sMMO | Methylocystis sp. WI 14 | ethanol + ethanal + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | ethene + NAD(P)H + O2 | sMMO | Methylocystis sp. | epoxyethane + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | ethene + NAD(P)H + O2 | sMMO | Methylocystis sp. WI 14 | epoxyethane + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | fluorobenzene + NAD(P)H + O2 | sMMO | Methylocystis sp. | fluorophenol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | heptane + NAD(P)H + O2 | sMMO | Methylocystis sp. | 1-heptanol + 2-heptanol + NAD(P)+ + H2O | position of hydroxylation cannot be determined exactly | ? | |
1.14.13.25 | hexane + NAD(P)H + O2 | sMMO | Methylocystis sp. | 1-hexanol + 2-hexanol + NAD(P)+ + H2O | position of hydroxylation cannot be determined exactly | ? | |
1.14.13.25 | methane + NAD(P)H + O2 | - |
Methylocystis sp. | methanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | methane + NAD(P)H + O2 | - |
Methylocystis sp. WI 14 | methanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylocystis sp. | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | additional information | sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity | Methylocystis sp. | ? | - |
? | |
1.14.13.25 | additional information | sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity | Methylocystis sp. WI 14 | ? | - |
? | |
1.14.13.25 | naphthalene + NAD(P)H + O2 | sMMO | Methylocystis sp. | alpha-naphthol + beta-naphthol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | pentane + NAD(P)H + O2 | sMMO | Methylocystis sp. | 1-pentanol + 2-pentanol + NAD(P)+ + H2O | position of hydroxylation cannot be determined exactly | ? | |
1.14.13.25 | propane + NAD(P)H + O2 | - |
Methylocystis sp. | 1-propanol + 2-propanol + NAD(P)+ + H2O | only 2-propanol, sMMO | ? | |
1.14.13.25 | propane + NAD(P)H + O2 | - |
Methylocystis sp. WI 14 | 1-propanol + 2-propanol + NAD(P)+ + H2O | only 2-propanol, sMMO | ? | |
1.14.13.25 | propylene + NAD(P)H + O2 | enzyme form sMMO | Methylocystis sp. | propylene oxide + NADP+ + H2O | - |
? | |
1.14.13.25 | toluene + NAD(P)H + H+ + O2 | sMMO | Methylocystis sp. | cresol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | xylene + NAD(P)H + O2 | sMMO | Methylocystis sp. | xylenol + NAD(P)+ + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.13.25 | ? | component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE | Methylocystis sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.25 | pMMO | particulate, membrane-bound enzyme form | Methylocystis sp. |
1.14.13.25 | sMMO | soluble, cytoplasmic enzyme form | Methylocystis sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | 7.2 | - |
assay at | Methylocystis sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | NADH | in vivo only NADH can be the electron donor | Methylocystis sp. | |
1.14.13.25 | NADPH | only in vitro | Methylocystis sp. |