3.5.1.2	arsenate	50 mM, 800% of the relative activity without addition	655601	
3.5.1.2	Ca2+	0.5-1.0 mM, 2fold activation of NEM-insensitive enzyme	209018	
3.5.1.2	chloride	competes with phosphate for binding to the catalytic Ser291, at high concentration (500 mM NaCl) it can dislodge phosphate from its site and shift the protein equilibrium to lower-order oligomers	720930	
3.5.1.2	Cl-	1 mM, markedly activates the enzyme	654234	
3.5.1.2	K+	110% activity at 1 mM	733562	
3.5.1.2	K+	139.43% activity at 100 mM	733133	
3.5.1.2	K+	5 mM, 113% of initial activity	755231	
3.5.1.2	KCl	2 M, 1.4fold activation	209032	
3.5.1.2	KCl	25% activation at 1 mM	669739	
3.5.1.2	additional information	equivalent activities in absence and the presence of 3 M NaCl	654091	
3.5.1.2	additional information	no effect with NaCl, no significant alteration with KCl, MgCl2, MnCl2, CaCl2 and NH4Cl	655601	
3.5.1.2	additional information	not influenced by Mg2+, Zn2+, and Ni2+	733562	
3.5.1.2	additional information	the enzyme from strain RIB40 is salt-tolerant, while the enzyme from strain MA-27-IM is salt-sensitive	669542	
3.5.1.2	additional information	the enzyme is not affected by NiCl2 at 1 mM	669739	
3.5.1.2	additional information	the enzyme is salt-tolerant, the C-terminally serine protease-cleaved enzyme fragment shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism	668534	
3.5.1.2	additional information	the enzyme is salt-tolerant, the C-terminally truncated enzyme shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism	667444	
3.5.1.2	Na+	1 mol/l: 2fold activity	701208	
3.5.1.2	Na+	10 mM, 129% of initial activity	754315	
3.5.1.2	Na+	120.35% activity at 100 mM	733133	
3.5.1.2	Na+	5 mM, 114% of initial activity	755231	
3.5.1.2	NaBr	0.25 M, 1.2-1.3fold activation	209032	
3.5.1.2	NaCl	5%, increases activity almost 2fold	655373	
3.5.1.2	NaCl	75% of the original activity in the presence of 15-30% NaCl	713385	
3.5.1.2	NaCl	8-16%, maximal activity of glutaminase I, no effect of glutaminase II	209026	
3.5.1.2	NaCl	enhances activity at 1-20% w/v, but reduces activity by 30% at 25% w/v, optimal at 1%	718613	
3.5.1.2	NaCl	enzyme is salt-tolerant as the relative activity displays 110% in the condition of 5% NaCl and remains over 50% in the presence of 20% NaCl	710791	
3.5.1.2	NaCl	enzyme retains 40% of its activity in the presence of 15% NaCl, which is about 2fold higher than the activity of glutaminase from Aspergillus oryzae	710869	
3.5.1.2	NaCl	optimum concentration 2%	753989	
3.5.1.2	NaCl	salt-tolerant, 110% relative activity under 5% NaCl, 50% activity at 15% (w/v) concentration, over 50% activity with presence of 20% NaCl	710911	
3.5.1.2	NaCl	the enzyme is salt-tolerant, over 86% of maximal activity at 16% NaCl, no effect at 1 mM	669739	
3.5.1.2	NaF	0.25 M, 1.2-1.3fold activation	209032	
3.5.1.2	NaI	0.25 M, 1.2-1.3fold activation	209032	
3.5.1.2	NH4+	Ka 1 mM	654884	
3.5.1.2	phosphate	50 mM, 900% of the relative activity without addition	655601	
3.5.1.2	phosphate	activates the enzyme in vivo in tumor cells at 100 mM	667496	
3.5.1.2	phosphate	induces association to form active tetramers	657262	
3.5.1.2	phosphate	no activity without phosphate, max. activity at 60 mM K3PO4	697985	
3.5.1.2	phosphate	phosphate-activated glutaminase isozyme	669694, 670129, 670391	
3.5.1.2	PO43-	143.13% activity at 100 mM	733133	
3.5.1.2	PO43-	activity increases with the increase of the concentration of the ion	654234	
3.5.1.2	sulfate	50 mM, 700% of the relative activity without addition	655601