EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.2.16 | Cd2+ |
apoenzyme reconstituted with Co2+ has 15.8fold lower activity than the native Zn-containing enzyme |
654421 |
| 3.5.2.16 | Co2+ |
apoenzyme reconstituted with Co2+ has about 2fold higher activity than the native Zn-containing enzyme |
654421 |
| 3.5.2.16 | Cobalt |
purified imidase, less the addition of any metals, reveals 0.514 mol zinc, 0.102 mol cobalt, and 0.179 mol nickel per subunit |
711007 |
| 3.5.2.16 | Mg2+ |
only the two physiological substrates dihydrouracil and dihydrothymine are hydrolyzed at a greater rate in the presence of 5 mM MgSO4 |
209268 |
| 3.5.2.16 | Mn2+ |
apoenzyme reconstituted with Co2+ has 4.4fold lower activity than the native Zn-containing enzyme |
654421 |
| 3.5.2.16 | more |
enzyme reconstituted with Cu2+ and Ni2+ has no enzymatic activity |
654421 |
| 3.5.2.16 | Nickel |
purified imidase, less the addition of any metals, reveals 0.514 mol zinc, 0.102 mol cobalt, and 0.179 mol nickel per subunit |
711007 |
| 3.5.2.16 | Zinc |
native enzyme contains 1 Zn2+ per subunit |
654421 |
| 3.5.2.16 | Zinc |
purified imidase, less the addition of any metals, reveals 0.514 mol zinc, 0.102 mol cobalt, and 0.179 mol nickel per subunit. Enzyme purified from cells grown in zinc-supplemented medium contain an approximate stoichiometric amount of the metal of 1.65 mol zinc per subunit. The activity of the apo-imidase depleted of zinc is recovered with the addition of zinc in the lower concentration of 0-20 micorM, whereas the enzymatic activity is decreased in the presence of high concentration of zinc above 100 microM |
711007 |
| 3.5.2.16 | Zn2+ |
residue C7 is required or binding of Zn2+ and maintaining the stability of the enzyme |
721108 |
