EC Number   |
Metals/Ions |
Reference |
|---|
   4.4.1.3 | Ca2+ |
- |
747144 |
| 4.4.1.3 | Cobalt |
DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM |
749057 |
| 4.4.1.3 | copper |
DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM |
749057 |
| 4.4.1.3 | Iron |
isolated protein contains 0.5 Fe per subunit. The UV-visible spectrum exhibits a feature at 550 nm, consistent with a tyrosinate-Fe(III) ligand-to-metal charge transfer transition. Both the Fe(III) oxidized and Fe(II) reduced species are active |
747110 |
| 4.4.1.3 | Iron |
the as-isolated enzyme contains 0.2-0.4 equivalents of bound iron. DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM, with Mn(II) and Fe(III) exhibiting weaker binding affinities. The presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme |
749057 |
| 4.4.1.3 | Manganese |
the presence of Fe(II) or Mn(II) elicits an about 40fold increase in DddW lyase activity compared to the apo-enzyme |
749057 |
| 4.4.1.3 | Mn2+ |
- |
747144 |
| 4.4.1.3 | more |
none of the metals Co, Cu, Mn, Ni or Zn is detected at above background levels |
716137 |
| 4.4.1.3 | Nickel |
DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM |
749057 |
| 4.4.1.3 | Zinc |
Zn2+ is bound at the active site |
748399 |
