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Literature summary extracted from

  • Tinberg, C.E.; Lippard, S.J.
    Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates H(peroxo) and Q proceed by distinct mechanisms (2010), Biochemistry, 49, 7902-7912.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.25 additional information
-
 additional information kinetics for class III substrates of Hperoxo, and kinetics and thermodynamic parameters for class III substrates of Q at 4°C and 20°C, overview Methylococcus capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.25 soluble
-
 Methylococcus capsulatus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.25 methane + NADH + H+ + O2 Methylococcus capsulatus
-
 methanol + H2O + NAD+
-
 ?
1.14.13.25 additional information Methylococcus capsulatus the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.25 0.3 0.45 pH 7.0, 45°C Methylococcus capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NADH + H+ + O2
-
 Methylococcus capsulatus methanol + H2O + NAD+
-
 ?
1.14.13.25 methanol + NADH + H+ + O2 substrate of intermediate species, Hperoxo and Q, kinetics, overview Methylococcus capsulatus ? + H2O + NAD+
-
 ?
1.14.13.25 methylamine + NADH + H+ + O2 substrate of intermediate species, Hperoxo and Q, kinetics, overview Methylococcus capsulatus hydroxymethylamine + H2O + NAD+
-
 ?
1.14.13.25 methylcyanide + NADH + H+ + O2 substrate of intermediate species, Hperoxo and Q, kinetics, and proposed mechanism of CH3CN hydroxylation by Hperoxo, overview Methylococcus capsulatus hydroxymethylcyanide + H2O + NAD+
-
 ?
1.14.13.25 additional information the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane Methylococcus capsulatus ?
-
 ?
1.14.13.25 additional information the enzyme catalyzes the selective oxidation of methane to methanol, but is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane. Reactions of the two intermediate species, of Hperoxo and Q, two oxidants that are generated sequentially during the reaction of reduced protein with O, with a panel of substrates of varying C-H bond strength, double-mixing stoppedflow spectroscopy, overview. Three classes of substrates exist according to the rate-determining step in the reaction Methylococcus capsulatus ?
-
 ?
1.14.13.25 propylaldehyde + NADH + H+ + O2 substrate of intermediate species, Hperoxo and Q, kinetics, overview Methylococcus capsulatus ? + H2O + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 MMO
-
 Methylococcus capsulatus
1.14.13.25 MMOH
-
 Methylococcus capsulatus
1.14.13.25 soluble methane monooxygenase
-
 Methylococcus capsulatus
1.14.13.25 soluble methane monooxygenase hydroxylase
-
 Methylococcus capsulatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.25 45
-
 assay at Methylococcus capsulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.25 7
-
 assay at Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 NADH
-
 Methylococcus capsulatus

General Information

EC Number General Information Comment Organism
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 Methylococcus capsulatus