EC Number |
Metals/Ions |
Reference |
---|
1.1.1.71 | NaCl |
the enzyme requires high salt concentrations for its activity, a preference for KCl over NaCl is observed |
728288 |
1.1.1.71 | Co2+ |
required |
737536 |
1.1.1.71 | Ca2+ |
Ca2+ has an stabilizing effect. With 1.0 mM CaCl2, the enzyme is completely stable at 0°C for 2 h and after 3.5 h almost 90% of the initial activity is retained |
740200 |
1.1.1.71 | Co2+ |
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol |
761529 |
1.1.1.71 | Fe2+ |
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol |
761529 |
1.1.1.71 | Fe3+ |
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol |
761529 |
1.1.1.71 | Mn2+ |
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol |
761529 |
1.1.1.71 | more |
no activity with Ca2+, Mg2+, Zn2+, and Cu2+. The Fe2+-reconstituted Ni-PhADH is sensitively and rapidly inactivated by dioxygen gas. The activity of apoform o-PhADH is significantly lower than that of Ni2+-bound PhADH. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs |
761529 |
1.1.1.71 | Ni2+ |
required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol |
761529 |