6.4.1.2	Ca2+	can partially replace for Mg2+	651169	
6.4.1.2	Co2+	26% of the maximum activity is observed when Co2+ (10 to 15 mM) is used as a divalent cation	725234	
6.4.1.2	Co2+	can partially replace for Mg2+	651169	
6.4.1.2	Cs+	dependent on	662786	
6.4.1.2	Cs+	greater activation at 1 mM HCO3- than at 10 mM HCO3-	37576	
6.4.1.2	Cs+	small activating effect, depends on the degree of saturation of the reaction by HCO3-	37577	
6.4.1.2	Cu2+	inhibitory for forward reaction, stimulates reverse reaaction	653435	
6.4.1.2	Fe2+	stimulates activity	653435	
6.4.1.2	Fe3+	stimulates activity	653435	
6.4.1.2	K+	activates	37578	
6.4.1.2	K+	dependent on	662786	
6.4.1.2	K+	greatest activation at 12-15 mM K+, at HCO3- concentration of 0.18 mM, 1 mM, and 10 mM	37576	
6.4.1.2	K+	small activating effect, depends on the degree of saturation of the reaction by HCO3-	37577	
6.4.1.2	Mg2+	-	37584, 660652, 660969, 661098, 664350, 665262, 665515, 665526, 666673, 691327, 691556, 693050, 693446, 693951, 694384, 695014, 702599, 705505	
6.4.1.2	Mg2+	about 10 mM Mg2+ required for maximal activity, inhibition above 15 mM	37580	
6.4.1.2	Mg2+	absolutely required for activity	662786	
6.4.1.2	Mg2+	activates	37591	
6.4.1.2	Mg2+	both MgATP2- and free Mg2+ required. Maximal activation at 5 mM Mg2+	37577	
6.4.1.2	Mg2+	complex with ATP	651638	
6.4.1.2	Mg2+	concentration of Mg2+ must be sufficient to allow chelation by both ATP and citrate. Free Mg2+ inhibits	37584	
6.4.1.2	Mg2+	dependent on	702459	
6.4.1.2	Mg2+	essential activator	37574	
6.4.1.2	Mg2+	free Mg2+ activates	37576	
6.4.1.2	Mg2+	maximal activation when ATP exists largely as MgATP2- with low concentrations of free Mg2+	37578	
6.4.1.2	Mg2+	maximal activity at 2 mM Mg2+ in presence of 1 mM ATP	37600	
6.4.1.2	Mg2+	maximal activity at 3 mM Mg2+ with 1 mM ATP and at 4 mM Mg2+ with 3 mM ATP	37576	
6.4.1.2	Mg2+	maximum acetyl-CoA carboxylase activity is obtained at 4.0 mM	725234	
6.4.1.2	Mg2+	Mg2+ or Mn2+ essential for activity	37577, 37594	
6.4.1.2	Mg2+	optimal concentration of 9686 enzyme: 5 mM, optimal concentration of Wayne enzyme: 3 mM	37574	
6.4.1.2	Mg2+	required	714212	
6.4.1.2	Mg2+	required to form a complex with ATP	651169	
6.4.1.2	Mg2+	required, maximum activity at 4 mM	745205	
6.4.1.2	Mg2+	the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis	664564	
6.4.1.2	Mn2+	1.0 mM Mn2+ gives 82% of the maximum activity obtained with the Mg2+ ion	725234	
6.4.1.2	Mn2+	20% of activation relative to Mg2+, at 2 mM	37600	
6.4.1.2	Mn2+	activates	37591	
6.4.1.2	Mn2+	can partially replace for Mg2+	651169	
6.4.1.2	Mn2+	maximal activity at 1 mM Mn2+ with 1 mM ATP. Maximal activity is 25% of that observed with Mg2+	37576	
6.4.1.2	Mn2+	maximal activity at 8 mM	37591	
6.4.1.2	Mn2+	Mn2+ or Mg2+ essential for activity. Maximal activation at 1.5 mM Mn2+	37577	
6.4.1.2	Mn2+	no effect	37574	
6.4.1.2	Mn2+	the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis	664564	
6.4.1.2	additional information	Fe2+, Cu2+, Ca2+, and Ni2+ (0.5 to 20 mM) have no effect on enzyme activity	745205	
6.4.1.2	additional information	the zinc domain in bacterial carboxyltransferase belongs to the zinc ribbon class of zinc fingers, Zn domains are commonly associated with DNA binding	695014	
6.4.1.2	NH4+	dependent on	662786	
6.4.1.2	NH4+	greater activation at 1 mM HCO3- than at 10 mM HCO3-	37576	
6.4.1.2	phosphate	contains 2.1 mol phosphate per 215000 g of protein	37586	
6.4.1.2	phosphate	contains 3.2 mol of phosphate per mol of subunit	37588	
6.4.1.2	phosphate	contains 9.83 mM of phosphate per mg of protein	37592	
6.4.1.2	phosphate	contains approximately 6 mol phosphate per 240000 g of protein	37585, 37590	
6.4.1.2	phosphate	dephosphorylation does not result in activation	37604	
6.4.1.2	phosphate	phosphate content of the 10000000 MW enzyme form: 4.0 mol of phosphate per mol of subunit. Phosphate content of the 2000000 MW enzyme form: 6.0 mol phosphate per mol of subunit. The 10000000 MW subunit and the 2000000 MW subunit are interconvertible by phosphorylation and dephosphorylation. Dephosphorylation by [acetyl-CoA carboxylase]-phosphatase 2 activates the enzyme and reduces its dependence on citrate	37571	
6.4.1.2	Zn2+	inhibitory for forward reaction, stimulates reverse reaaction	653435