EC Number   |
Metals/Ions |
Reference |
|---|
   1.8.3.7 | Ca2+ |
activation |
740770 |
| 1.8.3.7 | Ca2+ |
contains 2 Ca2+ ions |
742234 |
| 1.8.3.7 | Ca2+ |
contains two Ca2+ ions |
742836 |
| 1.8.3.7 | Ca2+ |
the enzyme requires a Ca2+ ion |
742835 |
| 1.8.3.7 | Cu(I) |
the enzyme (FGE) mediates O2-activation and hydrogen-atom abstraction in an active site that contains Cu(I) coordinated to two cysteine residues. The 1.04 A crystal structure of the enzyme in complex with copper and a cysteine-containing peptide substrate unveils a network of four crystallographic waters and two active site residues that form a highly acidic O2-binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(I) center |
764469 |
| 1.8.3.7 | Cu(I) |
the enzyme binds the substrate directly at a mononuclear Cu(I) center to initiate O2 activation. The copper atom is coordinated by two active-site cysteine residues in a nearly linear geometry |
765680 |
| 1.8.3.7 | Cu+ |
copper-metalloenzyme, one equivalent of Cu+ per acive site. No other transition metals can replace copper |
740316 |
| 1.8.3.7 | Cu+ |
CuSO4 and CuCl are almost equally efficient |
740309 |
| 1.8.3.7 | Cu+ |
required |
742288 |
| 1.8.3.7 | Cu2+ |
0.002 mM used in assay conditions |
742289 |
