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1.14.18.3: methane monooxygenase (particulate)

This is an abbreviated version!
For detailed information about methane monooxygenase (particulate), go to the full flat file.

Word Map on EC 1.14.18.3

Reaction

methane
+
quinol
+
O2
=
methanol
+
quinone
+
H2O

Synonyms

copper-containing membrane monooxygenase, copper-containing membrane-bound monooxygenase, CuMMO, membrane-associated methane monooxygenase, membrane-bound methane monooxygenase, membrane-embedded methane monooxygenase, methane hydroxylase, mMMO, MMO, particulate methane mono-oxygenase, particulate methane monooxygenas, particulate methane monooxygenase, particulate methane monooxygenase A, particulate methane-oxidizing complex, particulate MMO, PMH, pMMO, pMMO hydroxylase, pMMO-H, pMMO1, pMMO2, PmoA, PmoB, sMMO, soluble methane monooxygenase, spmoB

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.18.3 methane monooxygenase (particulate)

Purification

Purification on EC 1.14.18.3 - methane monooxygenase (particulate)

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by centrifugation and gel filtration
-
DEAE-Sepharose Fast Flow column chromatography, lysine agarose column chromatography, Sephacryl S-300HR gel filtration, QEA-Sephadex A-50 column chromatography, and Sephacryl S200 gel filtration, Superdex 200 gel filtration, or ammonium sulfate precipitation followed by Source 30Q column chroamtography
-
FPLC liquid chromatography and Mono Q HR 5/50 GL column chromatography
-
membrane-associated methane-oxidizing complex consisting of the particulate methane mono-oxygenase, pMMOH, and an unidentified component, assigned as a potential particulate methane mono-oxygenase reductase, pMMOR
-
MonoQ 10/100 GL column chromatography and Sephacryl S100 gel filtration
-
native enzyme from mebranes by solubilization with n-dodecyl beta-D-maltopyranoside, anion exchange chromatography, and ultrafiltration
-
native holoenzyme from isolated membranes by solubilization with detergent n-dodecyl beta-D-maltoside, ultrafiltration, and gel filtration
Ni2+-Sepharose Fast Flow column chromatography
-
optimization of solubilization and purification procedure for the hydroxylase component of membrane-bound enzyme, purification to homogeneity involves solubilization by dodexylbeta-D-maltoside, ion exchange chromatography and gel filtration, the purification includes the loss of the reductase component
-
partially by preparation of washed membranes
-
particulate form of methane hydroxylase (pMH) obtained by ion exchange and hydrophobic chromatography
-
pMMO after induction with copper, kinetic type I with respect to O2-sensitivity
-
POROS 20HQ column chromatography, gel filtration. Purified pMMO is inherently instable in vitro
-
stable and active native pMMO from membranes, by solubilization with 1% w/v CHAPS, removal of soluble proteins, gel filtration, anion exchange chromatography, and ultrafiltration
-