EC Number   |
Metals/Ions |
Reference  |
|---|
   1.13.11.24 | Cu |
probably belongs to the nonblue class, two atoms per molecule of enzyme |
439530, 439533 |
| 1.13.11.24 | Cu |
cupric ion |
439533 |
| 1.13.11.24 | Cu |
1-1.6 mol per mol enzyme, nonblue type 2 Cu2+ protein |
439535 |
| 1.13.11.24 | Cu |
0.8 mol per mol enzyme |
439537 |
| 1.13.11.24 | Cu |
Cu2+ |
439538 |
| 1.13.11.24 | Iron |
different coordination geometry in the two active sites of the dimer |
654768 |
| 1.13.11.24 | copper |
type II site |
654978 |
| 1.13.11.24 | copper |
single Cu(II) ion in active site |
656551 |
| 1.13.11.24 | Co2+ |
Co2+ salt addition increases the activity of quercetin 2,3-dioxygenase 24fold. The Escherichia coli cultures were grown at 37°C and 200 rpm for 6 h, induced with isopropyl beta-D-thiogalactopyanoside to a final concentraton of 50 mg/l in the presence of 10 microM CoCl2, and allow to grow additional 4 h at 25°C. The protein contains 0.65-0.8 atom of cobalt and 0.1 atom of iron per subunit. |
672046 |
| 1.13.11.24 | Cu2+ |
Cu2+ salt addition increases the activity of quercetin 2,3-dioxygenase 1.4fold. The Escherichia coli cultures were grown at 37°C and 200 rpm for 6 h, induced with isopropyl beta-D-thiogalactopyanoside to a final concentraton of 50 mg/l in the presence of 10 microM CuCl2, and allow to grow additional 4 h at 25°C. |
672046 |
