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