EC Number   |
Metals/Ions |
Reference  |
|---|
   1.10.3.1 | Co2+ |
1 mM, slight stimulation |
440427 |
| 1.10.3.1 | Cu+ |
1 mM, 234% activity |
440427 |
| 1.10.3.1 | Cu2+ |
1 mM, 241% activity, enzyme contains 0.24% copper |
440427 |
| 1.10.3.1 | Pb2+ |
1 mM, slight stimulation |
440427 |
| 1.10.3.1 | Zn2+ |
1 mM, slight stimulation |
440427 |
| 1.10.3.1 | Cu2+ |
type 3 copper enzyme, coordination number of 4 for each copper atom, CuII-CuII distance of 2.9 A |
440435 |
| 1.10.3.1 | more |
artificial dinuclear copper complexes as functional models for catechol oxidase |
440435 |
| 1.10.3.1 | Cu2+ |
binuclear copper center each coordinated by three histidine nitrogen atoms, in the oxidized enzyme structure the 2 copper II centers contain a hydroxide bridging group completing the four-coordinated trigonal pyramidal coordination sphere, in the reduced form the CuI-CuI separation increases to 4.4 A and a water molecule coordinates to one copper |
440439 |
| 1.10.3.1 | copper |
the copper centers in the protein are directly involved in the catechol oxidation |
657987 |
| 1.10.3.1 | Cu2+ |
active site binding |
671593 |
