2.3.3.13	Cd2+	-	702097	
2.3.3.13	Co2+	Co2+ is capable of supporting robust catalytic activity	718698	
2.3.3.13	Co2+	ratio kcat/Kact 0.052 per s and M. Detailed kinetic analysis	671604	
2.3.3.13	K+	-	636525	
2.3.3.13	K+	4 mM, slight stimulation	676632	
2.3.3.13	K+	an excess amount of 50 mM K+ is included in the standard enzymatic assays. Only isoform IPMS1 is coactivated by monovalent metal ions like K+	736457	
2.3.3.13	K+	enzyme activity increases 1.5fold in the presence of 100 mM KCl or NaCl	735677	
2.3.3.13	K+	enzyme requires the presence of monovalent cations, K+ is most effective	636532	
2.3.3.13	K+	K+ is the kinetically preferred ion	718698	
2.3.3.13	K+	K+ is the likely physiological allosteric activator	671604	
2.3.3.13	K+	Km: 80 mM, inhibitory at higher concentrations	5664	
2.3.3.13	K+	required	636520	
2.3.3.13	K+	strongly dependent on the presence of monovalent cations, K+ is most effective	5664	
2.3.3.13	K+	the activator interacts with the catalytic TIM barrel domain, it does not induce any significant effect on the enzyme structure	685842	
2.3.3.13	KCl	100 mM, activity is increased 1.5fold	727047	
2.3.3.13	Li+	can partially replace K+ in activation	5664	
2.3.3.13	Li+	stimulates at low concentrations	636525	
2.3.3.13	Mg2+	activates	735592	
2.3.3.13	Mg2+	and Mn2+, best activators, ratio kcat/Kact 0.014 per s and M. Detailed kinetic analysis	671604	
2.3.3.13	Mg2+	Mg2+ is capable of supporting robust catalytic activity	718698	
2.3.3.13	Mg2+	required, both isoforms IPMS1 and IPMS2	676632	
2.3.3.13	Mg2+	requires Mg2+ in millimolar concentrations	676632	
2.3.3.13	Mg2+	stimulates, maximal activity at 2 mM	636531	
2.3.3.13	Mn2+	1 mM, 25% activation	636516	
2.3.3.13	Mn2+	after treatment with EDTA, 4 mM Mn2+ restores about 50% of the initial activity	676632	
2.3.3.13	Mn2+	after tretment with EDTA, 4 mM Mn2+ restores about 50% of the initial activity	676632	
2.3.3.13	Mn2+	and Mg2+, best activators, ratio kcat/Kact 0.034 per s and M. Detailed kinetic analysis	671604	
2.3.3.13	Mn2+	contains two Mn2+ ion	718923	
2.3.3.13	Mn2+	contains two Mn2+ ions	718923	
2.3.3.13	Mn2+	Mn2+ is capable of supporting robust catalytic activity	718698	
2.3.3.13	Mn2+	most effective activator, an excess amount 2 mM Mn2+ is included in the standard enzymatic assays	736457	
2.3.3.13	additional information	enzyme contains a metal ion	636512, 636515	
2.3.3.13	additional information	the enzyme is active in the absence of exogenous monovalent or divalent metals. Addition of 1 mM EDTA results in a 96% decrease in activity, consistent with the requirement for divalent metals and suggesting that the enzyme is copurified with a divalent metal	727047	
2.3.3.13	additional information	the enzyme requires a divalent metal for activity and is activated by monovalent cations	718935	
2.3.3.13	Na+	enzyme activity increases 1.5fold in the presence of 100 mM KCl or NaCl	735677	
2.3.3.13	Na+	stimulates, maximal activity at 1 mM	636531	
2.3.3.13	NaCl	100 mM, activity is increased 1.5fold	727047	
2.3.3.13	NH4+	only isoform IPMS1 is coactivated by monovalent metal ions like NH4+	736457	
2.3.3.13	Rb+	activation	671604	
2.3.3.13	Rb+	can partially replace Rb+ in activation	5664	
2.3.3.13	Zinc	contains approximately 4 gatoms of zinc per dimer of 130000 Da	636514	
2.3.3.13	Zinc	enzyme of strain S288C contains 2 gatoms of zinc per subunit	636532	
2.3.3.13	Zn2+	-	702097	
2.3.3.13	Zn2+	contains one Zn2+ ion	718923