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	Co2+	required	737536	
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	K+	optimally active in the presence of 2 M KCl	722208	
1.1.1.71	KCl	600 mM, 147% of initial activity	726712	
1.1.1.71	KCl	a preference for KCl over NaCl is observed, with best activity at 4 M KCl	728288	
1.1.1.71	KCl	activity increases in the presence of KCl is maintained even at concentration of 3 M	726712	
1.1.1.71	KCl	maximally active with ethanol with 4 M KCl. It is maximally active with 1-propanol with 2 M KCl and with 1-butanol and 1-pentanol with 1 M KCl. Optimum activity with the secondary alcohols, 2-propanol and 2-butanol, is observed with 3 M KCl and 2 M KCl, respectively, and with isoamyl alcohol in the presence of 1 M KCl. Maximum activity with benzyl alcohol is detected with 2 M KCl. Catalyzed the reductive reaction optimally at pH 6.0 with 1 M KCl	726769	
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	additional information	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	additional information	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