Any feedback?
Literature summary extracted from
- Low-temperature biological activation of methane structure, function and molecular interactions of soluble and particulate methane monooxygenases (2017), Rev. Environ. Sci. Biotechnol., 16, 611-623 .
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | energy production | teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) | Methylococcus capsulatus |
| 1.14.18.3 | energy production | teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) | Methylococcus capsulatus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.13.25 | cytoplasm | - |
Methylococcus capsulatus | 5737 | - |
| 1.14.13.25 | cytoplasm | - |
Methylosinus trichosporium | 5737 | - |
| 1.14.13.25 | soluble | - |
Methylococcus capsulatus | - |
- |
| 1.14.18.3 | membrane | - |
Methylosinus trichosporium | 16020 | - |
| 1.14.18.3 | membrane | - |
Methylocystis sp. | 16020 | - |
| 1.14.18.3 | membrane | membrane-bound | Methylococcus capsulatus | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.25 | Fe2+ | the Fe2S2 domain of the reductase protein transfers electrons to carboxylate-bridged di-iron centers in the hydroxylase component of sMMO, structure of the Fe2S2 (ferredoxin) domain of sMMO reductase, overview. The Fe2S2 cluster is a di-iron pair coordinated by the sulfur atoms of cysteine residues 42, 47, 50, and 82 | Methylococcus capsulatus |  |
| 1.14.13.25 | Iron | soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation | Methylosinus trichosporium | |
| 1.14.18.3 | copper | the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylosinus trichosporium | |
| 1.14.18.3 | copper | the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. | |
| 1.14.18.3 | Cu2+ | required for activity, each of pmoA, pmoB, and pmoC houses a dicopper center | Methylococcus capsulatus | |
| 1.14.18.3 | additional information | the pMMO active site might possess a di-iron center located at the transmembrane zinc/copper site | Methylococcus capsulatus | |
| 1.14.18.3 | Zn2+ | enzyme-bound | Methylococcus capsulatus | |
Natural Substrates/ Products (Substrates)
| 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 | Methylosinus trichosporium | - |
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 | Methylococcus capsulatus Bath | - |
methanol + quinone + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.25 | Methylococcus capsulatus | - |
- |
- |
| 1.14.13.25 | Methylococcus capsulatus Bath | - |
- |
- |
| 1.14.13.25 | Methylosinus trichosporium | P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562 | P27353 (alpha/MmoX), P27355 (gamma/MmoZ), P27354 (beta/MmoY), P27356 (MmoB), Q53563 (MmoC), Q53562 (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 | 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 | Methylocystis sp. | - |
- |
- |
| 1.14.18.3 | Methylocystis sp. Rockwell | - |
- |
- |
| 1.14.18.3 | Methylosinus trichosporium | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.13.25 | methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O | reaction mechanism of enzyme sMMO. During methane oxidation, first, the regulatory protein docks at the alpha2beta2 interface of alpha2beta2gamma2 of hydroxylase and therefore triggering a conformational change in the alpha-subunit. Subsequently, the hydroxylase acts as a proton carrier allowing oxygen and methane interface with the di-iron center, overview | Methylococcus capsulatus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
| 1.14.13.25 | methane + NADH + H+ + O2 | - |
Methylosinus trichosporium | 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 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylosinus trichosporium | methanol + quinone + H2O | - |
? | |
| 1.14.18.3 | methane + quinol + O2 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. | methanol + quinone + H2O | - |
? | |
| 1.14.18.3 | methane + quinol + O2 | - |
Methylococcus capsulatus Bath | methanol + quinone + H2O | - |
? | |
| 1.14.18.3 | methane + quinol + O2 | methane activation occurs at the Cu centers of particulate methane monooxygenase | Methylocystis sp. Rockwell | methanol + quinone + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | More | structural architecture of sMMO, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site | Methylococcus capsulatus |
| 1.14.18.3 | heterotrimer | enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites | Methylococcus capsulatus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | sMMO | - |
Methylococcus capsulatus |
| 1.14.13.25 | sMMO | - |
Methylosinus trichosporium |
| 1.14.13.25 | soluble methane monooxygenase | - |
Methylococcus capsulatus |
| 1.14.13.25 | soluble methane monooxygenase | - |
Methylosinus trichosporium |
| 1.14.18.3 | particulate methane monooxygenase | - |
Methylosinus trichosporium |
| 1.14.18.3 | particulate methane monooxygenase | - |
Methylocystis sp. |
| 1.14.18.3 | particulate methane monooxygenase | - |
Methylococcus capsulatus |
| 1.14.18.3 | pMMO | - |
Methylosinus trichosporium |
| 1.14.18.3 | pMMO | - |
Methylocystis sp. |
| 1.14.18.3 | pMMO | - |
Methylococcus capsulatus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.25 | 20 | 25 | - |
Methylosinus trichosporium |
| 1.14.13.25 | 37 | - |
- |
Methylococcus capsulatus |
| 1.14.18.3 | 37 | - |
- |
Methylococcus capsulatus |
| 1.14.18.3 | 40 | 45 | - |
Methylosinus trichosporium |
| 1.14.18.3 | 40 | 45 | - |
Methylocystis sp. |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.25 | 6.5 | 7 | - |
Methylosinus trichosporium |
| 1.14.18.3 | 7.2 | 7.3 | - |
Methylosinus trichosporium |
| 1.14.18.3 | 7.2 | 7.3 | - |
Methylocystis sp. |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.25 | FAD | - |
Methylococcus capsulatus | |
| 1.14.13.25 | FAD | soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation | Methylosinus trichosporium | |
| 1.14.13.25 | additional information | the overall picture of the sMMO reductase reveals an electron pathway as NADH -> FAD -> [2Fe-2S] -> methane monohydroxylase (MMOH) | Methylococcus capsulatus | |
| 1.14.13.25 | NADH | - |
Methylococcus capsulatus | |
| 1.14.13.25 | NADH | soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation | Methylosinus trichosporium | |
| 1.14.13.25 | [2Fe-2S]-center | - |
Methylococcus capsulatus | |
| 1.14.18.3 | NAD+ | methane activation by particulate methane monooxygenase is NAD-dependent | Methylosinus trichosporium | |
| 1.14.18.3 | NAD+ | methane activation by particulate methane monooxygenase is NAD-dependent. Docking simulations of NAD+ on the enzyme clearly show preferential binding of the cofactor in the vicinity of the Cu metal centers confirming its functional relationship with particulate methane monooxygenase | Methylocystis sp. | |
| 1.14.18.3 | quinol | - |
Methylococcus capsulatus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.13.25 | additional information | analysis of structural and functional differences of sMMO and pMMO, EC 1.14.18.3, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview. Structural architecture of sMMO. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), structure-function relationships, detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site, sMMOH docking simulations. MMOB acts as a controller of the methane-to-methanol conversion reaction | Methylococcus capsulatus |
| 1.14.13.25 | physiological function | MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol | Methylococcus capsulatus |
| 1.14.18.3 | additional information | analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview | Methylococcus capsulatus |
| 1.14.18.3 | physiological function | MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol | Methylococcus capsulatus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
