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Literature summary for 1.14.13.25 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
Search for more literature for 1.14.13.25

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Methylococcus capsulatus

Crystallization (Commentary)

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
heterotrimer
-
 Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
MMOH
-
 Methylococcus capsulatus
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

Cofactor Comment Organism Structure
NADH
-
 Methylococcus capsulatus