2.4.1.90	Ca2+	10 mM used in assay conditions	757639	
2.4.1.90	Ca2+	about 50% of the activity with Mn2+	489555	
2.4.1.90	Ca2+	active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q	658032	
2.4.1.90	Ca2+	can partially replace Mn2+	489493	
2.4.1.90	Ca2+	slight activation	660309	
2.4.1.90	Co2+	activates, not as effective as Mn2+	660309	
2.4.1.90	Co2+	activation at 14.9% of the activity with Mn2+	489526	
2.4.1.90	Co2+	less active than Mn2+ with wild-type and mutant enzymes	658032	
2.4.1.90	Fe2+	no activation	489555	
2.4.1.90	Fe2+	partial activation	489555	
2.4.1.90	Mg2+	about 50% of the activity with Mn2+	489555	
2.4.1.90	Mg2+	activates, not as effective as Mn2+	660309	
2.4.1.90	Mg2+	active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q	658032	
2.4.1.90	Mg2+	can partially replace Mn2+	489493	
2.4.1.90	Mn2+	-	488947, 489501, 659804, 660308, 672411, 672454, 673897, 675468	
2.4.1.90	Mn2+	0.0025 mM required for half-maximal activity	489512	
2.4.1.90	Mn2+	1 mM used in assay conditions	756991	
2.4.1.90	Mn2+	10 mM used in assay conditions	757639	
2.4.1.90	Mn2+	100% activity at 1 mM	756911	
2.4.1.90	Mn2+	20 mM, stimulates	489543	
2.4.1.90	Mn2+	5 mM used in assay conditions	756352, 756430, 758173	
2.4.1.90	Mn2+	binding of two Mn(II) per mol of enzyme in the ternary enzyme-manganese-UDPgalactose complex. The affinity of the enzyme for manganese is much higher in the presence of UDPgalactose than in its absence	489524	
2.4.1.90	Mn2+	Km for MnCl2: 0.34 mM	489526	
2.4.1.90	Mn2+	Km: 0.03 mM	489520	
2.4.1.90	Mn2+	Km: 0.4 mM	489529	
2.4.1.90	Mn2+	maximal activity at 3-5 mM	488947	
2.4.1.90	Mn2+	maximal activity at 4 mM	489526	
2.4.1.90	Mn2+	no activation in presence of Fe2+, Zn2+ and Cu2+	489555	
2.4.1.90	Mn2+	optimal concentration 3-5 mM	488947	
2.4.1.90	Mn2+	optimal concentration is 10 mM	489496	
2.4.1.90	Mn2+	optimal concentration is 5-10 mM MnCl2	489522	
2.4.1.90	Mn2+	optimal concentration: 12.5 mM	489533, 489535	
2.4.1.90	Mn2+	required	489492, 489493, 489496, 489512, 489520, 489521, 489522, 489523, 489524, 489526, 489529, 489530, 489533, 489534, 489535, 489546, 489555, 675421, 736208	
2.4.1.90	Mn2+	required by full length wild-type enzyme	659700	
2.4.1.90	Mn2+	required by full length wild-type enzyme, coordination structure	659700	
2.4.1.90	Mn2+	required for maximal activity at 25 mM	660309	
2.4.1.90	Mn2+	required, binding site structure involving Met344 and Asp254, mechanism overview, binding results in conformational changes in the catalytic domain	658502	
2.4.1.90	Mn2+	required, binding site structure, binding results in conformational changes in the catalytic domain	658502	
2.4.1.90	Mn2+	required, metal binding site structure with an uncommon coordination to the Sdelta atom of Met344, the site is located in the hinge region of along flexible loop, which changes from open to closed conformation upon binding of Mn2+ and UDP-galactose creating an oligosaccharide binding site in the enzyme structure, effect occurs specifically with UDP-galactose, not with other UDP-sugars,overview	658032	
2.4.1.90	Mn2+	the catalytic domain of the enzyme has two metal binding sites, each with a distinct affinity. Site I binds Mn2+ with high affinity and does not bind Ca2+. Site II binds a variety of metal ions, including Ca2+. In the primary metal binding site the Mn2+ ion is coordinated to five ligands, two supplied by the phosphates of the sugar nucleotide and the other three by D254, H347 and M344	489556	
2.4.1.90	additional information	metal ion specificity of wild-type and mutant enzymes, overview	658032	
2.4.1.90	Sr2+	active only with mutant enzymes M334H and M344E, no activity with wild-type enzyme and mutants M344A, M344S, and M344Q	658032	
2.4.1.90	Zn2+	activation at 9.2% of the activity with Mn2+	489526	
2.4.1.90	Zn2+	less active than Mn2+ with wild-type and mutant enzymes	658032