EC Number   |
General Information |
Reference  |
|---|
   1.14.13.25 | physiological function |
pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain |
-, 702501 |
| 1.14.13.25 | physiological function |
soluble methane monooxygenase is a bacterial enzyme that converts methane to methanol at a carboxylate-bridged diiron center with exquisite control. The enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane |
711260 |
| 1.14.13.25 | physiological function |
the enzyme is strongly regulated by the availability of copper. Methanobactin produced by Methylosinus trichosporium OB3b plays a key role in controlling expression of MMO genes in this strain |
744100 |
| 1.14.13.25 | metabolism |
Methyloceanibacter methanicus {R-67174} is capable of oxidizing methane as sole source of carbon and energy using solely a soluble methane monooxygenase |
-, 744797 |
| 1.14.13.25 | metabolism |
Methyloferula stellata AR4 is an aerobic acidophilic methanotroph, which, in contrast to most known methanotrophs but similar to Methylocella spp., possesses only a soluble methane monooxygenase |
745039 |
| 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 |
-, 745389 |
| 1.14.13.25 | more |
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 |
-, 745389 |
| 1.14.13.25 | metabolism |
ammonia-supplied Methylosinus trichosporium OB3b containing soluble methane monooxygenase (sMMO) grow at the fastest rate, while the highest poly-beta-hydroxybutyrate content is obtained by transferring nitrate-supplied bacteria with the expression of particulate methane monooxygenase (pMMO) to nitrogen-free mineral salts (NFMS) + 0.005 mmol/l Cu medium |
745453 |
| 1.14.13.25 | metabolism |
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system |
-, 745535 |
| 1.14.13.25 | metabolism |
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO, EC 1.14.18.3, and soluble MMO, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview |
-, 745730 |
