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Literature summary extracted from

  • Lee, S.J.; McCormick, M.S.; Lippard, S.J.; Cho, U.S.
    Control of substrate access to the active site in methane monooxygenase (2013), Nature, 494, 380-384.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.25 regulatory protein MMOB the native regulatory protein MMOB is required for maximum enzyme activity Methylococcus capsulatus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.25 expressed in Escherichia coli Methylococcus capsulatus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.25 sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 15% PEG 20000 (w/v) Methylococcus capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus P22869 and P18798 and P11987 alpha subunit and beta subunit and gamma subunit
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.25 DEAE-Sepharose column chromatography, Q sepharose column chromatography, S-200 gel filtration, and S-300 gel filtration Methylococcus capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 propylene + NADH + H+ + O2
-
 Methylococcus capsulatus propylene oxide + NAD+ + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.25 heterotrimer
-
 Methylococcus capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 MMOH
-
 Methylococcus capsulatus
1.14.13.25 sMMO the enzyme contains three protein components, a 251 kDa hydroxylase (MMOH), a 38.6 kDa reductase (MMOR), and a 15.9 kDa regulatory protein (MMOB) required to couple electron consumption with substrate hydroxylation at the catalytic diiron center of MMOH Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 NADH
-
 Methylococcus capsulatus