EC Number |
Metals/Ions |
Reference |
---|
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 |
672049 |
1.14.13.25 | Cu2+ |
cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production) |
701759 |
1.14.13.25 | Cu2+ |
component C contains no copper |
438939 |
1.14.13.25 | Cu2+ |
copper genetically regulates the enzyme activity of the soluble and membrane-bound form |
438928, 438929 |
1.14.13.25 | Cu2+ |
copper-containing protein component contains one copper atom per molecule |
438921 |
1.14.13.25 | Cu2+ |
cytochrome component contains 0.3-0.8 atoms copper per molecule |
438921 |
1.14.13.25 | Cu2+ |
expression of the genes encoding sMMO and pMMO is regulated by copper ions, with sMMO expressed solely when copper is limiting |
703761 |
1.14.13.25 | Cu2+ |
metal-binding titrations of MMOD and copper |
765765 |
1.14.13.25 | Cu2+ |
the membrane-bound pMMO contains 4.8 Cu2+ ions per 100 kDa protomer the purified pMMO contains 1.4 Cu2+ ions per 100 kDa protomer, the enzyme contains a dinuclear copper center |
685262 |
1.14.13.25 | Cu2+ |
when allylthiourea is removed, sMMO activity is maintained for an additional 24 generations, albeit at a slightly lower level due to the presence of 0.0007 mM of Cu2+ in the feed medium |
704758 |