EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | protein MMOB | inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview | Methylococcus capsulatus | |
1.14.13.25 | protein MMOD | inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview | Methylococcus capsulatus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.25 | additional information | - |
additional information | thermodynamics, stopped-flow kinetics, time-course profiles for MMOH reduction by MMOR ferredoxin and by MMOR3e- | Methylococcus capsulatus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.13.25 | soluble | - |
Methylococcus capsulatus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Fe2+ | the [2Fe-2S] cofactor of MMOR is a one-electron carrier, the ferredoxin center must transfer two electrons sequentially to MMOH to reduce fully each diiron(III) hydroxylase active site, overview | Methylococcus capsulatus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NADH + O2 | Methylococcus capsulatus | - |
methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + O2 | Methylococcus capsulatus Bath | - |
methanol + NAD+ + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.25 | Methylococcus capsulatus | - |
- |
- |
1.14.13.25 | Methylococcus capsulatus Bath | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates | Methylococcus capsulatus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NADH + O2 | - |
Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + O2 | modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview | Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + O2 | modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview | Methylococcus capsulatus Bath | methanol + NAD+ + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.13.25 | More | enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview | Methylococcus capsulatus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.25 | sMMO | - |
Methylococcus capsulatus |
1.14.13.25 | soluble methane monooxygenase | - |
Methylococcus capsulatus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | 4 | - |
assay at | Methylococcus capsulatus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | 7 | - |
assay at | Methylococcus capsulatus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | FAD | - |
Methylococcus capsulatus | |
1.14.13.25 | Ferredoxin | several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview | Methylococcus capsulatus | |
1.14.13.25 | NADH | - |
Methylococcus capsulatus |