6.3.2.2	As3+	As3+ coordinately upregulates GCL catalytic subunit and GCL modifier subunit mRNA levels resulting in increased GCL subunit protein expression, holoenzyme formation, and activity. As3+ increases the rate of transcription of both the GCL catalytic subunit and GCL modifier subunit genes and induces the posttranscriptional stabilization of GCL modifier subunit mRNA. The antioxidant N-acetylcysteine abolishes As3+-induced GCL catalytic subunit expression and attenuates induction of GCL modifier subunit. As3+ induction of GCL catalytic subunit and GCL modifier subunit is also differentially regulated by the MAPK signaling pathways and occurrs independent of the Nrf1/2 transcription factors	703807	
6.3.2.2	Cu2+	2 divalent metal ions per enzyme molecule are bound, can be replaced by Mn2+ and Mg2+, binding mechanism and kinetics, overview	652341	
6.3.2.2	Cu2+	induces expression of heavy subunit	651393	
6.3.2.2	K+	absolute requirement for Mg2+, Mn2+, and K+ ions	706061	
6.3.2.2	Mg2+	-	1126, 650713, 651896, 690385, 690440, 690630, 691909, 691912, 692055, 692058, 692442, 692444, 694060, 694485, 694609, 694674	
6.3.2.2	Mg2+	2 divalent metal ions per enzyme molecule are bound, Mg2+ sharpens the substrate specificity, increases the resistance to L-buthionine-S,R-sulfoximine, can be replaced by Mn2+ and Cu2+, binding mechanism and kinetics, overview	652341	
6.3.2.2	Mg2+	absolute requirement for Mg2+, Mn2+, and K+ ions	706061	
6.3.2.2	Mg2+	absolute requirement, maximal activity at 30-50 mM	1149	
6.3.2.2	Mg2+	divalent metal ion required, especially Mg2+, optimal concentration depending on ATP concentration	1120	
6.3.2.2	Mg2+	inactive in absence of Mg2+, maximal activity at 10 mM	1126	
6.3.2.2	Mg2+	Mg2+ or Mn2+ are required	650135	
6.3.2.2	Mg2+	required	672367, 694060, 726910, 726912, 744070, 744122, 744469, 744853, 745490, 745492, 745734, 745745, 745805, 745888, 745900	
6.3.2.2	Mg2+	required as MgATP2-	650634	
6.3.2.2	Mg2+	required, best at 20 mM	744438	
6.3.2.2	Mg2+	required, bound as MgATP2-, the metal ion specificity is determined by the second binding site n2 which also is involved in ATP binding, located in the active site and formed by 3 conserved residues Glu53, Gln321, and Glu489, Mg2+ can partly be substituted by Mn2+	652192	
6.3.2.2	Mg2+	required, bound to the erythrocyte enzyme	649263	
6.3.2.2	Mg2+	required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by 25%	649263	
6.3.2.2	Mg2+	required, bound to the kidney enzyme, involved in enzyme phosphorylation, can be substituted by Mn2+ by only 25%	649263	
6.3.2.2	Mn2+	2 divalent metal ions per enzyme molecule are bound, Mg2+ broadens the substrate specificity, decreases the resistance to L-buthionine-S,R-sulfoximine, can be replaced by Mg2+ and Cu2+, binding mechanism and kinetics, overview	652341	
6.3.2.2	Mn2+	absolute requirement for Mg2+, Mn2+, and K+ ions	706061	
6.3.2.2	Mn2+	bound to the erythrocyte enzyme	649263	
6.3.2.2	Mn2+	bound to the kidney enzyme, can substitute for Mg2+ by 25%	649263	
6.3.2.2	Mn2+	bound to the kidney enzyme, can substitute for Mg2+ by only 25%	649263	
6.3.2.2	Mn2+	can partly substitute for Mg2+	652192	
6.3.2.2	Mn2+	can replace Mg2+ with 18% of the efficiency	1126	
6.3.2.2	Mn2+	Mg2+ or Mn2+ are required	650135	
6.3.2.2	additional information	the first metal binding site n1 binds free metal ions and is composed of 3 conserved residues Glu55, Glu93, and Glu100, n1 also is involved in positioning of L-glutamate for the reaction, located in the active site	652192	
6.3.2.2	sodium arsenite	induces expression of heavy subunit	651393	
6.3.2.2	Zn2+	induces expression of heavy subunit	651393