Crystallization (Comment) | Organism |
---|---|
enzyme sMMO crystal structure analysis, PDB ID 1MTY | Methylococcus capsulatus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Methylococcus capsulatus | 5737 | - |
soluble | - |
Methylococcus capsulatus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | enzyme sMMO contains a non-heme diiron active site | Methylococcus capsulatus | |
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 | |
additional information | the enzyme does not contain and require Cu2+ for activity | Methylococcus capsulatus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
251000 | - |
- |
Methylococcus capsulatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NADH + H+ + O2 | Methylococcus capsulatus | - |
methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | Methylococcus capsulatus Bath | - |
methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | Methylococcus capsulatus Bath. | - |
methanol + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylococcus capsulatus | - |
- |
- |
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) | - |
Methylococcus capsulatus Bath | - |
- |
- |
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) | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NAD(P)H + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD(P)+ + H2O | - |
? | |
methane + NAD(P)H + H+ + O2 | - |
Methylococcus capsulatus Bath. | methanol + NAD(P)+ + H2O | - |
? | |
methane + NADH + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | - |
Methylococcus capsulatus Bath. | methanol + NAD+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |
Synonyms | Comment | Organism |
---|---|---|
sMMO | - |
Methylococcus capsulatus |
soluble methane monooxygenase | - |
Methylococcus capsulatus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Methylococcus capsulatus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |