EC Number |
Metals/Ions |
Reference |
---|
1.1.1.71 | KCl |
maximum activity in presence of 4 M KCl |
728288 |
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 |
metal independency is supported by the absence of a significant effect of TsAdh319 preincubation with 10 mM Me2+ for 30 min before measuring the activity in the presence of 1 mM Me2+ or EDTA |
726712 |
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 | NaCl |
400 mM, 206% of initial activity |
726712 |
1.1.1.71 | NaCl |
activity increases in the presence of NaCl is maintained even at concentration of 4 M |
726712 |
1.1.1.71 | NaCl |
activity is increased in the presence of NaCl and remains at the elevated level up to 4 M of NaCl. The rates of 2-propanol and 2,5-hexanediol oxidation are increased by more than 2fold after the addition of NaCl up to 1 M to the assay mixture and is retained at the increased level up to 4 M of NaCl |
726699 |
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 | Ni2+ |
required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol |
761529 |