6.4.1.4	Co2+	activates with 57% of the efficiency relative to Mg2+	1896	
6.4.1.4	Co2+	divalent cation required, Co2+ activates at 34% of the efficiency relative to Mg2+	1884	
6.4.1.4	Co2+	requirement for free Mg2+ ions can be partially replaced by Mn2+ or Co2+, but not by Zn2+	653128	
6.4.1.4	Cs+	activator	653128	
6.4.1.4	Cs+	monovalent cations activate, K+, Cs+, Rb+ or NH4+	1896	
6.4.1.4	K+	1.1 to 1.2fold stimulation in presence of 20 mM KCl. Inhibition at concentrations higher than 50 mM	1894	
6.4.1.4	K+	activated 4 to 5fold by K+ or NH4+, 50-100 mM, kidney enzyme	1885	
6.4.1.4	K+	activates 7fold at 50 mM. Relative activation by monovalent cations in decreasing order: K+/ NH4+, Na+, Li+	1884	
6.4.1.4	K+	activator	653128	
6.4.1.4	K+	monovalent cations activate, K+, Cs+, Rb+ or NH4+	1896	
6.4.1.4	Li+	relative activation by monovalent cations in decreasing order: K+/ NH4+, Na+, Li+	1884	
6.4.1.4	Mg2+	-	656207, 692864, 693791, 694194	
6.4.1.4	Mg2+	carboxylation of methylcrotonyl-CoA is Mg2+-dependent	653013	
6.4.1.4	Mg2+	divalent cation required, Mg2+ is the best activator	1884, 1896	
6.4.1.4	Mg2+	divalent metal ion required, maximal activity at 6 mM Mg2+	1895	
6.4.1.4	Mg2+	maximal activation at 2.5 mM Mg2+ in presence of 1 mM ATP	1894	
6.4.1.4	Mg2+	maximal activation at 3 mM Mg2+ in presence of 1 mM ATP	1894	
6.4.1.4	Mg2+	maximal activity at 2 mM Mg2+, at ATP concentrations 0.025 mM, 0.05 mM or 1 mM	1896	
6.4.1.4	Mg2+	Mg-ATP-dependent carboxylation	653498	
6.4.1.4	Mg2+	Mg2+ or Mn2+ required	1882	
6.4.1.4	Mg2+	Mg2+ required	1894	
6.4.1.4	Mg2+	requires free Mg2+ ions for activation, in excess of thatrequired to complex ATP	653128	
6.4.1.4	Mn2+	activates with 77% of the efficiency relative to Mg2+	1896	
6.4.1.4	Mn2+	divalent cation required. Mn2+ activates with 85% of the efficiency relative to Mg2+	1884	
6.4.1.4	Mn2+	Mn2+ or Mg2+ required	1882	
6.4.1.4	Mn2+	requirement for free Mg2+ ions can be partially replaced by Mn2+ or Co2+, but not by Zn2+	653128	
6.4.1.4	Na+	relative activation by monovalent cations in decreasing order: K+/ NH4+, Na+, Li+	1884	
6.4.1.4	NH4+	activated 4 to 5fold by K+ or NH4+, 50-100 mM, kidney enzyme	1885	
6.4.1.4	NH4+	activator	653128	
6.4.1.4	NH4+	monovalent cations activate, K+, Cs+, Rb+ or NH4+	1896	
6.4.1.4	NH4+	relative activation by monovalent cations in decreasing order: K+/ NH4+, Na+, Li+	1884	
6.4.1.4	Rb+	activator	653128	
6.4.1.4	Rb+	monovalent cations activate, K+, Cs+, Rb+ or NH4+. Maximal activity obtained with Rb+	1896