4.1.3.1	Ba2+	Ba2+ less effective activator than Mg2+	33121, 33153, 33155	
4.1.3.1	Ba2+	no activation	33147, 33148	
4.1.3.1	Ba2+	partial reactivation after thermal inactivation	33129	
4.1.3.1	Cd2+	5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, fluorescence spectra, and glutaraldehyde crosslinking)	701127	
4.1.3.1	Co2+	activating	664083	
4.1.3.1	Co2+	can partly replace Mg2+	638504	
4.1.3.1	Co2+	can replace Mg2+	651215	
4.1.3.1	Co2+	Co2+ 12% as effective as Mg2+	33140	
4.1.3.1	Co2+	Co2+ 17% as effective as Mg2+	33117	
4.1.3.1	Co2+	Co2+ 18% as effective as Mg2+	33141	
4.1.3.1	Co2+	Co2+ 29% as effective as Mg2+	33139	
4.1.3.1	Co2+	no activity in absence of exogenous cation	33117, 33139, 33140, 33141	
4.1.3.1	Fe2+	activating	664083	
4.1.3.1	Fe2+	no activity in absence of exogenous cation, Fe2+ 7% as effective as Mg2+	33140	
4.1.3.1	Mg2+	-	33131, 33134, 33138	
4.1.3.1	Mg2+	10 mM, dependent	638504, 651215	
4.1.3.1	Mg2+	5 mM, essential for catalytic activity, 100% activity, binds and stabilizes non-catalytic alpha/beta barrel core without structural alterations (revealed by thermal, urea and GdnHCL denaturation and far-UV CD)	701127	
4.1.3.1	Mg2+	absolute requirement	33135	
4.1.3.1	Mg2+	activating oxalacetate hydrolase activity	664083	
4.1.3.1	Mg2+	activity dependent on Mg2+	663832	
4.1.3.1	Mg2+	activity of demetallized enzyme: 0.5%	33147	
4.1.3.1	Mg2+	dependent	653939	
4.1.3.1	Mg2+	dependent on Mg2+	679815	
4.1.3.1	Mg2+	essential for activity, optimal concentration 3 mM	33121	
4.1.3.1	Mg2+	Icl enzyme: most effective cation, optimal concentration: 5 mM	651648	
4.1.3.1	Mg2+	ICL1, dependent on	702178	
4.1.3.1	Mg2+	increase of activity	33124, 33129, 33130, 33136, 33137, 33138, 33139, 33140, 33148	
4.1.3.1	Mg2+	isoform ICL1 is activated 3fold by 5 mM Mg2+	748480	
4.1.3.1	Mg2+	maximal activity at 3.7 mM	33138	
4.1.3.1	Mg2+	maximal activity at 5 mM	33138	
4.1.3.1	Mg2+	maximal activity at 5-6 mM	33138	
4.1.3.1	Mg2+	maximal activity at 6 mM	33138	
4.1.3.1	Mg2+	maximal activity at 8 mM	33153	
4.1.3.1	Mg2+	no activity in absence of exogenous cation, Mg2+ most effective	33117	
4.1.3.1	Mg2+	non-essential activator	33155	
4.1.3.1	Mg2+	reactivation after thermal inactivation, Mg2+-isocitrate complex is true substrate, 2 Mg2+-binding sites: catalytic and activator site	33122	
4.1.3.1	Mg2+	required	681995, 727039, 727045	
4.1.3.1	Mg2+	required for full activity, optimal concentration 5 mM	33141	
4.1.3.1	Mg2+	required, in the absence of Mg2+, no enzymatic activity is measured	748615	
4.1.3.1	Mg2+	requirement, optimal concentration: 2 mM, Km value: 0.092 at pH 7	649454	
4.1.3.1	Mn2+	5 mM, 45% activity, binds and stabilizes non-catalytic alpha/beta barrel core without structural alterations (revealed by thermal, urea and GdnHCL denaturation and far-UV CD)	701127	
4.1.3.1	Mn2+	activating oxalacetate hydrolase activity	664083	
4.1.3.1	Mn2+	can partly replace Mg2+	638504, 651215	
4.1.3.1	Mn2+	can replace Mg2+ with 24% of the activity of Mg2+	649454	
4.1.3.1	Mn2+	Icl enzyme: can replace Mg2+, yielding 39% of the activity obtained with Mg2+	651648	
4.1.3.1	Mn2+	ICL2 and ICL, dependent on	702178	
4.1.3.1	Mn2+	isoform ICL2 is activated 3fold by 5 mM Mn2+	748480	
4.1.3.1	Mn2+	Mn2+ 14% as effective as Mg2+	33140	
4.1.3.1	Mn2+	Mn2+ 24% as effective as Mg2+	33139	
4.1.3.1	Mn2+	Mn2+ 27% as effective as Mg2+	33148	
4.1.3.1	Mn2+	Mn2+ 30% as effective as Mg2+	33147	
4.1.3.1	Mn2+	Mn2+ 31% as effective as Mg2+	33141	
4.1.3.1	Mn2+	Mn2+ 54% as effective as Mg2+	33117	
4.1.3.1	Mn2+	Mn2+ less effective activator than Mg2+	33124, 33153, 33155	
4.1.3.1	Mn2+	no activity in absence of exogenous cation	33117, 33139, 33140, 33141, 33148	
4.1.3.1	Mn2+	partial reactivation after thermal inactivation	33129	
4.1.3.1	additional information	isoform ICL2 is not activated by Mg2+. Ca2+and K+ reveal no marked effect on both isoforms of the enzyme	748480	
4.1.3.1	additional information	no significant change in enzyme activity after incubation with Co2+, Pb2+, Fe2+, Cu2+, Cd2+, Na+, K+, Cl-	664147	
4.1.3.1	Ni2+	can partly replace Mg2+	638504, 651215	
4.1.3.1	Ni2+	less efficient activator than Mg2+	33155	
4.1.3.1	Ni2+	no activity in absence of exogenous cation, Ni2+ 7% as effective as Mg2+	33117	
4.1.3.1	Sr2+	no activation	33147, 33148	
4.1.3.1	Sr2+	no activity in absence of exogenous cation, Sr2+ 3% as effective as Mg2+	33117	
4.1.3.1	Zn2+	5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, ANS fluorescence spectra, and glutaraldehyde crosslinking)	701127