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Literature summary for 1.14.13.25 extracted from
- Methane monooxygenase hydroxylase and B component interactions (2006), Biochemistry, 45, 2913-2926.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A115C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| A62C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview, the mutant MMOH-MMOB complex is perturbed by salts but not nonionic detergents | Methylosinus trichosporium |
| D71C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| D87C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| G119C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| K15C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| K44C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| R133C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| S109C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| T111C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| V39C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| V68C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
| Y102C | site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview | Methylosinus trichosporium |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics | Methylosinus trichosporium |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| [2Fe-2S] cluster | bound to the MMOR enzyme component | Methylosinus trichosporium |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methane + NAD(P)H + O2 | Methylosinus trichosporium | - |
methanol + NAD(P)+ + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylosinus trichosporium | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methane + NAD(P)H + O2 | - |
Methylosinus trichosporium | methanol + NAD(P)+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | interaction of the soluble methane monooxygenase regulatory component, MMOB, and the active site-bearing hydroxylase component, MMOH, spin labeling with 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy, high affinity of labeled MMOB for the oxidized MMOH decreases substantially with increasing pH and increasing ionic strength but is nearly unaffected by addition of nonionic detergents, the MMOB-MMOH complex is stabilized by electrostatic interactions, overview | Methylosinus trichosporium |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| sMMO | - |
Methylosinus trichosporium |
| soluble methane monooxygenase | - |
Methylosinus trichosporium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Methylosinus trichosporium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Methylosinus trichosporium |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | bound to the MMOR enzyme component | Methylosinus trichosporium | |
| NADH | - |
Methylosinus trichosporium | |
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