EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.3 | NDH-2 | type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview | Methylococcus capsulatus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.13.25 | enzyme sMMO crystal structure analysis, PDB ID 1MTY | Methylococcus capsulatus |
1.14.18.3 | enzyme pMMO crystal structure analysis, PDB ID 3RGB | Methylococcus capsulatus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.13.25 | cytoplasm | - |
Methylococcus capsulatus | 5737 | - |
1.14.13.25 | soluble | - |
Methylococcus capsulatus | - |
- |
1.14.18.3 | membrane | membrane-bound | Methylococcus capsulatus | 16020 | - |
1.14.18.3 | membrane | membrane-bound | Methylocystis sp. M | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | Fe2+ | enzyme sMMO contains a non-heme diiron active site | Methylococcus capsulatus | |
1.14.13.25 | Iron | the diiron active site of each homodimer is located in the alpha subunit, and no other metal centers are present. The resting state active site (MMOHox) consists of two Fe(III) ions coordinated by Glu114, His147, and a solvent molecule (Fe1), and Glu209, Glu243, and His246 (Fe2). The iron ions are 3.1 A apart, coordinated in pseudooctahedral fashion and bridged by two solvent molecules as well as Glu144 | Methylococcus capsulatus | |
1.14.13.25 | additional information | the enzyme does not contain and require Cu2+ for activity | Methylococcus capsulatus | |
1.14.18.3 | copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylococcus capsulatus | |
1.14.18.3 | copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylosinus trichosporium | |
1.14.18.3 | copper | the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron | Methylocystis sp. | |
1.14.18.3 | Cu2+ | required for activity, enzyme pMMO has a copper active site. dicopper site occupied with a two copper ions or b one copper ion from Methylocystis speciesstrain M, structure comparisons, modeling | Methylocystis sp. M | |
1.14.18.3 | Cu2+ | required for activity, enzyme pMMO has a copper active site. Subdomain with a Cu-Cu distance of about 2.5 A, ligated by the N-terminal amino group and side chain of His33 (Cu1) as well as His137 and His139 (Cu2), and a zinc ion in PmoC about 20 A away from the PmoB dicopper site and attributed to the crystallization solution | Methylococcus capsulatus | |
1.14.18.3 | Zn2+ | binds in the copper active site | Methylococcus capsulatus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.13.25 | 251000 | - |
- |
Methylococcus capsulatus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NADH + H+ + O2 | Methylococcus capsulatus | - |
methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | Methylococcus capsulatus Bath | - |
methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | Methylococcus capsulatus Bath. | - |
methanol + NAD+ + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | Methylococcus capsulatus | - |
methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | Methylocystis sp. M | - |
methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | Methylococcus capsulatus Bath | - |
methanol + quinone + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.25 | Methylococcus capsulatus | - |
- |
- |
1.14.13.25 | Methylococcus capsulatus | P22869 and P18798 and P11987 and P18797 and P22868 and P22867 | P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD) | - |
1.14.13.25 | Methylococcus capsulatus Bath | - |
- |
- |
1.14.13.25 | Methylococcus capsulatus Bath. | P22869 and P18798 and P11987 and P18797 and P22868 and P22867 | P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD) | - |
1.14.18.3 | Methylococcus capsulatus | - |
- |
- |
1.14.18.3 | Methylococcus capsulatus | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
1.14.18.3 | Methylococcus capsulatus Bath | G1UBD1 AND Q607G3 | alpha- and beta-subunits | - |
1.14.18.3 | Methylococcus capsulatus Bath. | - |
- |
- |
1.14.18.3 | Methylocystis sp. | - |
- |
- |
1.14.18.3 | Methylocystis sp. M | - |
- |
- |
1.14.18.3 | Methylocystis sp. Rockwell | - |
- |
- |
1.14.18.3 | Methylosinus trichosporium | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | reaction mechanism and reaction cycle of enzyme sMMO, via O2 activation intermediates, detailed overview | Methylococcus capsulatus | |
1.14.18.3 | methane + quinol + O2 = methanol + quinone + H2O | reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview | Methylococcus capsulatus | |
1.14.18.3 | methane + quinol + O2 = methanol + quinone + H2O | reaction mechanism of enzyme pMMO, via O2 activation intermediates, detailed overview | Methylocystis sp. M |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.25 | methane + NAD(P)H + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | methane + NAD(P)H + H+ + O2 | - |
Methylococcus capsulatus Bath. | methanol + NAD(P)+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD+ + H2O | - |
? | |
1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylococcus capsulatus Bath. | methanol + NAD+ + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | - |
Methylococcus capsulatus | methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | - |
Methylocystis sp. M | methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + quinol + O2 | - |
Methylococcus capsulatus Bath | methanol + quinone + H2O | - |
? | |
1.14.18.3 | methane + reduced acceptor + H* + O2 | - |
Methylococcus capsulatus | methanol + acceptor + H2O | - |
? | |
1.14.18.3 | methane + reduced acceptor + H* + O2 | - |
Methylococcus capsulatus Bath | methanol + acceptor + H2O | - |
? | |
1.14.18.3 | methane + succinate + O2 | membrane-bound enzyme only | Methylococcus capsulatus | methanol + fumarate + H2O | - |
? | |
1.14.18.3 | methane + succinate + O2 | membrane-bound enzyme only | Methylococcus capsulatus Bath | methanol + fumarate + H2O | - |
? | |
1.14.18.3 | additional information | activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples | Methylococcus capsulatus | ? | - |
? | |
1.14.18.3 | additional information | activity assays on membrane-bound pMMO routinely utilize NADH, succinate, or duroquinol as reductant, while only duroquinol and to a lesser extent, other quinols, are effective for solubilized and purified samples | Methylococcus capsulatus Bath | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.13.25 | More | enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview | Methylococcus capsulatus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.25 | sMMO | - |
Methylococcus capsulatus |
1.14.13.25 | soluble methane monooxygenase | - |
Methylococcus capsulatus |
1.14.18.3 | pMMO | - |
Methylococcus capsulatus |
1.14.18.3 | pMMO | - |
Methylosinus trichosporium |
1.14.18.3 | pMMO | - |
Methylocystis sp. |
1.14.18.3 | pMMO | - |
Methylocystis sp. M |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.25 | NADH | - |
Methylococcus capsulatus | |
1.14.18.3 | quinol | - |
Methylococcus capsulatus | |
1.14.18.3 | quinol | - |
Methylocystis sp. M |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.13.25 | evolution | methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available | Methylococcus capsulatus |
1.14.13.25 | additional information | enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview | Methylococcus capsulatus |
1.14.18.3 | evolution | methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available | Methylococcus capsulatus |
1.14.18.3 | evolution | methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available | Methylocystis sp. M |
1.14.18.3 | additional information | enzyme pMMO contains a copper active site, active site structure, overview | Methylocystis sp. M |
1.14.18.3 | additional information | enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-Oยท) species | Methylococcus capsulatus |
1.14.18.3 | physiological function | methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO) | Methylococcus capsulatus |
1.14.18.3 | physiological function | methane monooxygenase (MMO) enzymes activate O2 for oxidation of methane. Two distinct MMOs exist in nature, a soluble form that uses a diiron active site (sMMO) and a membrane-bound form with a catalytic copper center (pMMO) | Methylocystis sp. M |