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- Methane_monooxygenase abstract "Methane monooxygenase, or MMO, is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes (EC 1.14.13.25). There are two well-studied forms of MMO: the soluble form (sMMO) and the particulate form (pMMO). The active site in sMMO contains a di-iron center bridged by an oxygen atom (Fe-O-Fe), whereas the active site in pMMO utilizes copper, although some propose that pMMO also uses iron. Structures of both proteins have been determined by X-ray crystallography; however, the location and mechanism of the active site in pMMO is still poorly understood and is an area of active research.The particulate methane monooxygenase and related ammonia monooxygenase are integral membrane proteins, occurring in methanotrophs and ammonia oxidisers, respectively, which are thought to be related. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of substrates including ammonia, methane, halogenated hydrocarbons, and aromatic molecules. These enzymes are composed of 3 subunits - A (IPR003393), B (IPR006833) and C (IPR006980) - and contain various metal centers, including copper. Particulate methane monooxygenase from Methylococcus capsulatus is an ABC homotrimer, which contains mononuclear and dinuclear copper metal centers, and a third metal center containing a metal ion whose identity in vivo is not certain.The A subunit from Methylococcus capsulatus (Bath) resides primarily within the membrane and consists of 7 transmembrane helices and a beta-hairpin, which interacts with the soluble region of the B subunit. A conserved glutamate residue is thought to contribute to a metal center.Methane monooxygenases are found in methanotrophic bacteria, a class of bacteria that exist at the interface of aerobic (oxygen-containing) and anaerobic (oxygen-devoid) environments. One of the more widely-studied bacteria of this type is Methylococcus capsulatus (Bath). This bacterium was discovered in the hot springs of Bath, England.".
- Methane_monooxygenase symbol "pMMO".
- Methane_monooxygenase thumbnail 1yew_opm.gif?width=300.
- Methane_monooxygenase wikiPageID "4423830".
- Methane_monooxygenase wikiPageRevisionID "606443652".
- Methane_monooxygenase hasPhotoCollection Methane_monooxygenase.
- Methane_monooxygenase interpro "IPR003393".
- Methane_monooxygenase name "Particulate methane monooxygenase".
- Methane_monooxygenase opmFamily "23".
- Methane_monooxygenase opmProtein "1".
- Methane_monooxygenase pdb "F:2-246".
- Methane_monooxygenase pfam "PF02461".
- Methane_monooxygenase symbol "pMMO".
- Methane_monooxygenase subject Category:EC_1.14.13.
- Methane_monooxygenase subject Category:Enzymes.
- Methane_monooxygenase subject Category:Integral_membrane_proteins.
- Methane_monooxygenase subject Category:Metalloproteins.
- Methane_monooxygenase subject Category:Oxidoreductases.
- Methane_monooxygenase type Abstraction100002137.
- Methane_monooxygenase type Activator114723079.
- Methane_monooxygenase type Catalyst114723628.
- Methane_monooxygenase type Chemical114806838.
- Methane_monooxygenase type Compound114818238.
- Methane_monooxygenase type Enzyme114732946.
- Methane_monooxygenase type Enzymes.
- Methane_monooxygenase type IntegralMembraneProteins.
- Methane_monooxygenase type Macromolecule114944888.
- Methane_monooxygenase type Material114580897.
- Methane_monooxygenase type Matter100020827.
- Methane_monooxygenase type Molecule114682133.
- Methane_monooxygenase type OrganicCompound114727670.
- Methane_monooxygenase type Part113809207.
- Methane_monooxygenase type PhysicalEntity100001930.
- Methane_monooxygenase type Protein114728724.
- Methane_monooxygenase type Relation100031921.
- Methane_monooxygenase type Substance100019613.
- Methane_monooxygenase type Thing100002452.
- Methane_monooxygenase type Unit109465459.
- Methane_monooxygenase type Biomolecule.
- Methane_monooxygenase type Protein.
- Methane_monooxygenase type BiologicalObject.
- Methane_monooxygenase comment "Methane monooxygenase, or MMO, is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes (EC 1.14.13.25). There are two well-studied forms of MMO: the soluble form (sMMO) and the particulate form (pMMO). The active site in sMMO contains a di-iron center bridged by an oxygen atom (Fe-O-Fe), whereas the active site in pMMO utilizes copper, although some propose that pMMO also uses iron.".
- Methane_monooxygenase label "Metano monoossigenasi".
- Methane_monooxygenase label "Metano monooxigenasa".
- Methane_monooxygenase label "Methan-Monooxygenase".
- Methane_monooxygenase label "Methane monooxygenase".
- Methane_monooxygenase label "Метанмонооксигеназа".
- Methane_monooxygenase label "メタンモノオキシゲナーゼ".
- Methane_monooxygenase sameAs Methan-Monooxygenase.
- Methane_monooxygenase sameAs Metano_monooxigenasa.
- Methane_monooxygenase sameAs Metano_monoossigenasi.
- Methane_monooxygenase sameAs メタンモノオキシゲナーゼ.
- Methane_monooxygenase sameAs m.0c1kq2.
- Methane_monooxygenase sameAs Q417187.
- Methane_monooxygenase sameAs Q417187.
- Methane_monooxygenase sameAs Methane_monooxygenase.
- Methane_monooxygenase wasDerivedFrom Methane_monooxygenase?oldid=606443652.
- Methane_monooxygenase depiction 1yew_opm.gif.
- Methane_monooxygenase isPrimaryTopicOf Methane_monooxygenase.
