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Literature summary for 1.14.18.3 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)

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Fe2+ As-isolated enzyme conatins 1.31 Fe2+ equivalents per 100 kDa pMMO Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-
Methylococcus capsulatus Bath
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
particulate methane monooxygenase
-
Methylococcus capsulatus
pMMO
-
Methylococcus capsulatus