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Literature summary extracted from

  • Sirajuddin, S.; Barupala, D.; Helling, S.; Marcus, K.; Stemmler, T.L.; Rosenzweig, A.C.
    Effects of zinc on particulate methane monooxygenase activity and structure (2014), J. Biol. Chem., 289, 21782-21794 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.18.3 purified native enzyme, sitting drop vapour diffusion method, mixing of 0.0025 ml of 20 mg/ml pMMO protein, and 0.0005 ml of 85 mM n-octyl beta-D-thiomaltoside with 0.002 ml of 10% PEG 3000, 200 mM magnesium formate dihydrate, 100 mM sodium cacodylate trihydrate, pH 6.5, at room temperature, 1-4 weeks, for the complex structure, the crystals are soaked in Zn2+ solution, X-ray diffraction structure determination and analysis at 2.6 A resolution Methylocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.18.3 Zn2+ effects of zinc binding on pMMO in membrane extracts, binding efficiency varies under different consitions, multisite inhibition, detailed overview. Addition of copper to these zinc-loaded membranes results in loss of half the zinc ions Methylococcus capsulatus
1.14.18.3 Zn2+ zinc inhibits enzyme pMMO at two sites that are distinct from the copper active site, zinc might inhibit proton transfer in pMMO. Locations for the two zinc inhibition sites: the first is the crystallographic zinc site in the pmoC subunit, a second zinc site is present on the cytoplasmic side of the pmoC subunit Methylocystis sp.

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.3 Cu2+ required Methylocystis sp.
1.14.18.3 Cu2+ required, preferred metal ion Methylococcus capsulatus
1.14.18.3 additional information metal content of Methylococcus capsulatus (Bath) crude membranes before (as-isolated) and after (apo) cyanide treatment, and of apo-membranes after zinc and zinc/copper loading, overview. When zinc is loaded first, copper can replace one zinc site, which is likely the more accessible pmoC site. The activity of the zinc- and copper-loaded membrane-bound pMMO is 11-18% of the copper-reconstituted membrane-bound pMMO activity. This activity is lower than the 40-60% observed for copper- and zinc-loaded pMMO, even though the metal stoichiometries are similar, which is consistent with zinc occupying the active site when loaded first Methylococcus capsulatus
1.14.18.3 additional information the final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule Methylocystis sp.
1.14.18.3 Zn2+ can replace Cu2+, enzyme-bound, structure analysis, overview. Zinc binding at the pmoC site in the zinc-soaked structure stabilizes pmoC residues 200-210 Methylococcus capsulatus
1.14.18.3 Zn2+ enzyme bound, structure analysis, overview Methylocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.18.3 100000
-
 about Methylococcus capsulatus
1.14.18.3 450000
-
 about, enzyme complex, native PAGE Methylocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.3 methane + quinol + O2 Methylocystis sp.
-
 methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2 Methylococcus capsulatus
-
 methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2 Methylococcus capsulatus Bath
-
 methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2 Methylocystis sp. Rockwell
-
 methanol + quinone + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.3 Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
-
1.14.18.3 Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-
1.14.18.3 Methylocystis sp.
-
-
-
1.14.18.3 Methylocystis sp. Rockwell
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.18.3 native enzyme from mebranes by solubilization with n-dodecyl beta-D-maltopyranoside, anion exchange chromatography, and ultrafiltration Methylocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.3 methane + duroquinol + O2
-
 Methylocystis sp. methanol + duroquinone + H2O
-
 ?
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 methane + duroquinol + O2
-
 Methylocystis sp. Rockwell methanol + duroquinone + H2O
-
 ?
1.14.18.3 methane + NADH + O2
-
 Methylococcus capsulatus methanol + NAD+ + H2O
-
 ?
1.14.18.3 methane + NADH + O2
-
 Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylocystis sp. methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus Bath methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylocystis sp. Rockwell methanol + quinone + H2O
-
 ?
1.14.18.3 additional information methane oxidation activity of apo membrane-bound Methylococcus capsulatus (Bath) pMMO after metal loading using two copper reconstitution methods, overview Methylococcus capsulatus ?
-
 ?
1.14.18.3 additional information methane oxidation activity of apo membrane-bound Methylococcus capsulatus (Bath) pMMO after metal loading using two copper reconstitution methods, overview Methylococcus capsulatus Bath ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.18.3 heterotrimer three pMMO subunits confirmed by mass spectrometry Methylocystis sp.
1.14.18.3 heterotrimer three pMMO subunits confirmed by mass spectrometry Methylococcus capsulatus
1.14.18.3 More three-dimensional structure determination and analysis Methylocystis sp.

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.18.3 22
-
 assay at room temperature Methylocystis sp.
1.14.18.3 22
-
 assay at room temperature Methylococcus capsulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.18.3 7 7.2 assay at Methylocystis sp.
1.14.18.3 7 7.2 assay at Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.18.3 duroquinol
-
 Methylocystis sp.
1.14.18.3 duroquinol NADH passes electron to duroquinol Methylococcus capsulatus

General Information

EC Number General Information Comment Organism
1.14.18.3 additional information nano-LC-ESI-MS/MS analysis for protein identification of purified Methylocystis sp. str. Rockwell pMMO. The final model for the zinc-soaked structure included pmoB residues 29-418, pmoA residues 9-252, and pmoC residues 16-210 and 224-256, three polyalanine helices consisting of up to 25 residues, five zinc ions, three copper ions, and one cacodylate molecule Methylocystis sp.