2.4.1.19	(NH4)6Mo7O24	5 mM, 115% of initial activity	718610	
2.4.1.19	Ba2+	-	488861	
2.4.1.19	Ba2+	0.5 mM, 125% of initial activity	719222	
2.4.1.19	Ba2+	activates	684517	
2.4.1.19	Ba2+	INMIA 3849, stabilizes enzyme	488855	
2.4.1.19	BaCl2	relative activity 102.4%	488839	
2.4.1.19	Ca2+	-	488826, 488831, 488836, 488839, 488855, 488863, 736253	
2.4.1.19	Ca2+	0.5 mM, 116% of initial activity	719222	
2.4.1.19	Ca2+	4 mM CaCl2, relative activity 106%	488836	
2.4.1.19	Ca2+	5 mM, 120% of initial activity	718610	
2.4.1.19	Ca2+	about 110% activity at 1 mM	758476	
2.4.1.19	Ca2+	activates	689822	
2.4.1.19	Ca2+	activates at 10 mM	684942	
2.4.1.19	Ca2+	addition increases thermal stability	488826, 488831	
2.4.1.19	Ca2+	contains 1 mol Ca2+ per mol of enzyme	488839	
2.4.1.19	Ca2+	contains 2 mol Ca2+ per mol of enzyme, increases heat stability, denaturation temperature shifted from 70°C to 88°C	488839	
2.4.1.19	Ca2+	protects enzyme from activity loss	488842, 488861	
2.4.1.19	Ca2+	raise the unfolding temperature of CGTase	701849	
2.4.1.19	Ca2+	required	758336	
2.4.1.19	Ca2+	slight activating effect (113% activity at 10 mM)	737302	
2.4.1.19	Ca2+	synergistic promoting effects of glycine and Ca2+ on the extracellular secretion of the recombinant protein in Escherichia coli, optimal at 150 mM and 20 mM, respectively, overview	704134	
2.4.1.19	Ca2+	the enzyme has three Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability	736290	
2.4.1.19	Ca2+	the enzyme has two Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability	736290	
2.4.1.19	Ca2+	the highest increase in beta-CGTase activity is 54.3% at 1 mM CaCl2 which is 5.6fold higher than that of the control. The highest increase in gamma-CGTase activity is 55.5% 1 mM CaCl2 which is 7.2fold higher than that of the control	758261	
2.4.1.19	Ca2+	thermal stability is remarkably increased by addition of calcium ions	488847, 488853, 488863	
2.4.1.19	CaCl2	5 mM, 20% activation of cross-linked enzyme crystals, 2% activation of soluble enzyme	659739	
2.4.1.19	CaCl2	activates at 1 mM	684450	
2.4.1.19	CaCl2	relative activity 106.7%	488839	
2.4.1.19	Cd2+	about 110% activity at 1 mM	758476	
2.4.1.19	Co2+	10 mM, 28% inhibition	673390	
2.4.1.19	Co2+	activates	684517, 684523	
2.4.1.19	CoCl2	activates at 4 mM	684450	
2.4.1.19	Cu2+	-	488861	
2.4.1.19	Cu2+	10 mM, 20% inhibition	673390	
2.4.1.19	Cu2+	5% enhancement of activity at 1 mM Cu2+	735782	
2.4.1.19	Cu2+	about 108% activity at 1 mM	758476	
2.4.1.19	Cu2+	activates	684523	
2.4.1.19	Cu2+	INMIA 3849, stabilizes enzyme	488855	
2.4.1.19	Fe2+	-	488861	
2.4.1.19	Fe2+	10 mM, 58% inhibition	673390	
2.4.1.19	Fe2+	9% enhancement of activity at 1 mM Fe2+	735782	
2.4.1.19	Fe2+	INMIA 3849, stabilizes enzyme	488855	
2.4.1.19	FeCl2	1 mM, 89.3% activation	660343	
2.4.1.19	FeCl2	5 mM, 110% activation of cross-linked enzyme crystals, inhibition of soluble enzyme	659739	
2.4.1.19	FeSO4	relative activity 107.6%	488839	
2.4.1.19	Hg2+	10 mM, complete inhibition	673390	
2.4.1.19	K+	5 mM, 110% of initial activity	718610	
2.4.1.19	K+	80 mM KCl, relative activity 112%	488836	
2.4.1.19	Li+	about 118% activity at 10 mM	758476	
2.4.1.19	Li2SO4	relative activity 106%	488839	
2.4.1.19	Mg2+	10 mM used in assay conditions	756738	
2.4.1.19	Mg2+	10 mM, 75% inhibition	673390	
2.4.1.19	Mg2+	about 130% activity at 10 mM	758476	
2.4.1.19	Mg2+	activates	684523	
2.4.1.19	Mg2+	protects enzyme from activity loss	488861	
2.4.1.19	Mg2+	the enzymatic activity increases to 104.1% in the presence of 5 mM MgCl2	757110	
2.4.1.19	Mg2+	the highest increase in beta-CGTase activity is 46.4% at 2 mM MgSO4 which is 4.8fold higher than that of the control. The highest increase in gamma-CGTase activity is 45.9% at 3 mM MgSO4 which is 5.9fold higher than that of the control	758261	
2.4.1.19	MgSO4	relative activity 103.2%	488839	
2.4.1.19	Mn2+	about 115% activity at 1 mM	758476	
2.4.1.19	Mn2+	activates	684517, 684523, 688313	
2.4.1.19	Mn2+	the enzymatic activity increases to 104.1% in the presence of 5 mM MnCl2	757110	
2.4.1.19	additional information	enzyme activity is not affected by Ca2+, Na+, K+, Fe3+, ICH2COOH, and SDS at low concentration	684523	
2.4.1.19	additional information	Ni2+ and Na+ ions have weak effects on the enzyme activity	737302	
2.4.1.19	additional information	not influenced by 5 mM Ba2+	757110	
2.4.1.19	Na+	5 mM, 120% of initial activity	718610	
2.4.1.19	Na+	80 mM NaCl, relative activity 110%	488836	
2.4.1.19	Ni2+	about 140% activity at 10 mM	758476	
2.4.1.19	Sr2+	activates	684523	
2.4.1.19	Zn2+	0.5 mM, 118% of initial activity	719222	
2.4.1.19	Zn2+	10 mM, 65% inhibition	673390