2.4.1.65	Ba2+	stimulates	637635	
2.4.1.65	Ca2+	can replace Mn2+ for activation, optimum concentration is 10-15 mM	660797	
2.4.1.65	Ca2+	leads to 2.1fold activation of SFT3	661313	
2.4.1.65	Ca2+	stimulates	637635	
2.4.1.65	Cd2+	stimulates	637635	
2.4.1.65	Co2+	leads to 2.8fold activation of SFT3	661313	
2.4.1.65	Co2+	stimulates	637635	
2.4.1.65	Cu2+	no significant activity is detected	661313	
2.4.1.65	Mg2+	can replace Mn2+ for activation, optimum concentration is 10-15 mM	660797	
2.4.1.65	Mg2+	leads to 2.5fold activation of SFT3	661313	
2.4.1.65	Mg2+	required for activity	661845	
2.4.1.65	Mg2+	stimulates, 20 mM required for maximal activation	637635	
2.4.1.65	Mn2+	-	637636, 658008, 693000	
2.4.1.65	Mn2+	absolutely required	691644	
2.4.1.65	Mn2+	activation above pH 8.0	637636	
2.4.1.65	Mn2+	binds the enzyme and increases affinity for the acceptor. One possible functional role of manganese in catalysis can be as an electrophilic catalyst, co-ordinating the negative charges of the phosphate groups of the GDP-Fuc donor and promoting Fuc transfer. A low pH values such role would be played by the proton. Mn2+ leads to 2.7fold activation of SFT3	661313	
2.4.1.65	Mn2+	Fuc-T V is Mn2+ dependent	661341	
2.4.1.65	Mn2+	required for activation in vitro, optimum concentration is 10-15 mM	660797	
2.4.1.65	Mn2+	required for activity	661845	
2.4.1.65	Mn2+	stimulates, activation is maximal at 5 mM	637635	
2.4.1.65	additional information	Cu2+ inactivates the enzyme	660797	
2.4.1.65	additional information	FUT10 functions well without MnCl2	704613	
2.4.1.65	additional information	FUT11 functions well without MnCl2	704613	
2.4.1.65	additional information	the enzyme retains approximately 35% of its maximal activity in the absence of metal ions	661313	
2.4.1.65	Ni2+	stimulates	637635	
2.4.1.65	Zn2+	can replace Mn2+ for activation, but shows only half the maximal activity, optimum concentration is 10-15 mM	660797	
2.4.1.65	Zn2+	leads to 80% inhibition of STF3	661313	
2.4.1.65	Zn2+	stimulates	637635