Literature summary for 1.14.18.3 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 .

Search for more literature for 1.14.18.3

Crystallization (Commentary)

Crystallization (Comment)	Organism
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.

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
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
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

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

Metals/Ions

Metals/Ions	Comment	Organism
Cu2+	required	Methylocystis sp.
Cu2+	required, preferred metal ion	Methylococcus capsulatus
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
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.
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
Zn2+	enzyme bound, structure analysis, overview	Methylocystis sp.

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

General Information

General Information	Comment	Organism
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.