Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ukaegbu, U.E.; Henery, S.; Rosenzweig, A.C.
    Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase (2006), Biochemistry, 45, 10191-10198.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.25 soluble soluble enzyme, sMMO Methylococcus capsulatus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.25 copper the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.25 methane + NADH + O2 Methylococcus capsulatus
-
methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2 Methylococcus capsulatus Bath
-
methanol + NAD+ + H2O
-
?
1.14.13.25 additional information Methylococcus capsulatus the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview ?
-
?
1.14.13.25 additional information Methylococcus capsulatus Bath the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylococcus capsulatus
-
-
-
1.14.13.25 Methylococcus capsulatus Bath
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NADH + O2
-
Methylococcus capsulatus methanol + NAD+ + H2O
-
?
1.14.13.25 methane + NADH + O2
-
Methylococcus capsulatus Bath methanol + NAD+ + H2O
-
?
1.14.13.25 additional information the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview Methylococcus capsulatus ?
-
?
1.14.13.25 additional information the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview Methylococcus capsulatus Bath ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 particulate methane monooxygenase
-
Methylococcus capsulatus
1.14.13.25 pMMO
-
Methylococcus capsulatus
1.14.13.25 sMMO
-
Methylococcus capsulatus
1.14.13.25 soluble methane monooxygenase
-
Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 NADH
-
Methylococcus capsulatus