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Literature summary extracted from

  • Smith, S.M.; Balasubramanian, R.; Rosenzweig, A.C.
    Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit (2011), Methods Enzymol., 495, 195-210.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.18.3 expressed in Escherichia coli BL21(DE3) or Rosetta (DE3) pLysS cells Methylococcus capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.18.3 membrane
-
 Methylococcus capsulatus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.3 Cu2+ pMMO contains a dicopper center and a mononuclear copper center, As-isolated enzyme conatins 10.2 Cu2+ equivalents per 100 kDa pMMO Methylococcus capsulatus
1.14.18.3 Fe2+ As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO Methylococcus capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.3 Methylococcus capsulatus
-
-
-
1.14.18.3 Methylococcus capsulatus Bath
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.3 methane + duroquinol + O2
-
 Methylococcus capsulatus methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + duroquinol + O2
-
 Methylococcus capsulatus Bath methanol + duroquinone + H2O
-
 ?
1.14.18.3 propylene + duroquinol + O2
-
 Methylococcus capsulatus propylene oxide + duroquinone + H2O
-
 ?
1.14.18.3 propylene + duroquinol + O2
-
 Methylococcus capsulatus Bath propylene oxide + duroquinone + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.18.3 particulate methane monooxygenase
-
 Methylococcus capsulatus
1.14.18.3 pMMO
-
 Methylococcus capsulatus