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Literature summary extracted from

  • Zhang, J.; Wallar, B.J.; Popescu, C.V.; Renner, D.B.; Thomas, D.D.; Lipscomb, J.D.
    Methane monooxygenase hydroxylase and B component interactions (2006), Biochemistry, 45, 2913-2926.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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
1.14.13.25 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.25 additional information
-
 additional information steady-state kinetics Methylosinus trichosporium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.25 [2Fe-2S] cluster bound to the MMOR enzyme component Methylosinus trichosporium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.25 methane + NAD(P)H + O2 Methylosinus trichosporium
-
 methanol + NAD(P)+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylosinus trichosporium
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NAD(P)H + O2
-
 Methylosinus trichosporium methanol + NAD(P)+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.25 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

EC Number Synonyms Comment Organism
1.14.13.25 sMMO
-
 Methylosinus trichosporium
1.14.13.25 soluble methane monooxygenase
-
 Methylosinus trichosporium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.25 25
-
 assay at Methylosinus trichosporium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.25 7.6
-
 assay at Methylosinus trichosporium

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 FAD bound to the MMOR enzyme component Methylosinus trichosporium
1.14.13.25 NADH
-
 Methylosinus trichosporium