EC Number   |
Metals/Ions |
Reference |
|---|
    1.1.1.1 | Ba2+ |
1 mM, 113% of initial activity |
735498 |
| 1.1.1.1 | Ca2+ |
0.5 mM, substrate glycolaldehyde, 86.2% residual activity |
739927 |
| 1.1.1.1 | Ca2+ |
CaCl2 and MgCl2 are able to stabilize the enzyme at millimolar concentrations. Ca2+ stabilizes yeast ADH I by preventing the dissociation of the reduced form of the enzyme and by preventing the unfolding of the oxidized form of the enzyme. Ca2+ is fixed by the Asp236 and Glu101 side chains in yeast ADH I |
735629 |
| 1.1.1.1 | Ca2+ |
insertion of an RTX domain from the adenylate cyclase of Bordetella pertussis into a loop near the catalytic active site of the thermostable alcohol dehydrogenase D from Pyrococcus furiosus. The resultant chimera, beta-AdhD, gains the calcium-binding ability of the beta-roll, retains the thermostable activity of AdhD, and exhibits reduced overall alcohol dehydrogenase activity. The addition of calcium to beta-AdhD preferentially inhibits NAD+-dependent activity in comparison to NADP+-dependent activity. Calcium is a competitive inhibitor of AdhD, and the addition of the RTX domain introduces calcium-dependent noncompetitive inhibition to beta-AdhD affecting NAD+-dependent activity |
743908 |
| 1.1.1.1 | Co2+ |
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview |
655741 |
| 1.1.1.1 | Co2+ |
stimulation |
735360 |
| 1.1.1.1 | copper |
contains 0.5 mol of copper per mol of enzyme |
285580 |
| 1.1.1.1 | Cu2+ |
0.25 mM, substrate glycolaldehyde, no residual activity |
739927 |
| 1.1.1.1 | Cu2+ |
1 mM CuSO4, 1.7fold activation |
688442 |
| 1.1.1.1 | Cu2+ |
construction of an active metal-substituted mutant by substituting Zn2+ for Cu2+ or Co2+, which maintain the same configuration as the native zinc ion, but possessing a wider pH range and a lower activity and substrate affinity than the wild-type enzyme, overview |
655741 |
