3.6.1.23	Co2+	activates to 72% of the activity with Mg2+	670775	
3.6.1.23	Co2+	can partially replace Mg2+, causes increase in Km	657286	
3.6.1.23	Co2+	can substitute the physiological cofactor Mg2+, however the kcat is significantly reduced compared to dUTP-Mg2+	696412	
3.6.1.23	Co2+	strictly dependent on a bivalent metal cation like Co2+	718787	
3.6.1.23	Mg2+	-	667399, 667783, 669790, 669804, 670909, 685380, 686744, 689949	
3.6.1.23	Mg2+	0.5 mM, stimulates by 7%	209977	
3.6.1.23	Mg2+	5 mM used in assay conditions	756317	
3.6.1.23	Mg2+	activates	696282, 699236	
3.6.1.23	Mg2+	activates, phosphate chain coordination involves Mg2+, binding structure, overview. Mg2+ probably dissociates from the enzyme with the product PPi and not with dUMP	695290	
3.6.1.23	Mg2+	best divalent cation, bound at the center of the trimeric enzyme structure	670091