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Literature summary extracted from

  • Liew, E.
    Mutagenesis of the hydrocarbon monooxygenase indicates a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity (2014), Microbiology, 160, 1267-1277 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.18.3 crystal structure analysis, PDB ID 3CHX, structure modeling Methylosinus trichosporium

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.3 Cu2+ a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity Methylosinus trichosporium
1.14.18.3 Cu2+ a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity Methylocystis sp.
1.14.18.3 Cu2+ two metal sites: a dicopper centre coordinated by histidine residues in subunit-B and a variable-metal site coordinated by carboxylate and histidine residues from subunit-C. A metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity Methylococcus capsulatus

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 Methylosinus trichosporium
-
-
-

Subunits

EC Number Subunits Comment Organism
1.14.18.3 More enzyme structure comparisons, overview Methylosinus trichosporium
1.14.18.3 More enzyme structure comparisons, overview Methylocystis sp.
1.14.18.3 More enzyme structure comparisons, overview Methylococcus capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.14.18.3 copper-containing membrane monooxygenase
-
Methylosinus trichosporium
1.14.18.3 copper-containing membrane monooxygenase
-
Methylocystis sp.
1.14.18.3 copper-containing membrane monooxygenase
-
Methylococcus capsulatus
1.14.18.3 particulate methane monooxygenase
-
Methylosinus trichosporium
1.14.18.3 particulate methane monooxygenase
-
Methylocystis sp.
1.14.18.3 particulate methane monooxygenase
-
Methylococcus capsulatus
1.14.18.3 pMMO
-
Methylosinus trichosporium
1.14.18.3 pMMO
-
Methylocystis sp.
1.14.18.3 pMMO
-
Methylococcus capsulatus

General Information

EC Number General Information Comment Organism
1.14.18.3 evolution the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily Methylosinus trichosporium
1.14.18.3 evolution the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily Methylocystis sp.
1.14.18.3 evolution the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily Methylococcus capsulatus
1.14.18.3 additional information structure-function relationship of copper-containing membrane monooxygenases Methylosinus trichosporium
1.14.18.3 additional information structure-function relationship of copper-containing membrane monooxygenases Methylocystis sp.
1.14.18.3 additional information structure-function relationship of copper-containing membrane monooxygenases Methylococcus capsulatus