6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	determination of reaction and substrate binding mechanisms, large conformational changes in the catalytic cycle	653899	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	mechanism, active site residues are Glu144, Asn146, Lys305, and Lys364, interaction of these residues with the ligands is essential for enzyme activity, especially Glu144 seems to be very important for stabilization of the reaction intermediate, but the active site residues are not essential for the overall enzyme structure	652539	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	random ter-reactant reaction mechanism, overview	726912	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	residues A534 and A535 are involved in substrate binding and determination of substrate specificity	648904	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	substrate binding kinetics and mechanism, negative cooperativity of gamma-L-Glu-L-Cys	649553	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	the catalytic mechanism is proposed to proceed via phosphorylation of the dipeptide substrate to yield an acyl phosphate intermediate. This intermediate is subsequently attacked by glycine, followed by loss of inorganic phosphate, leading to glutathione formation	-, 1219	
6.3.2.3	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione	the reaction process involves the formation of an acyl phosphate on the cysteinyl moiety in L-gamma-glutamyl-L-cysteine, followed by the attack of the glycine and formation of an enzyme-product complex, which finally dissociates with the release of GSH, ADP and phosphate	727638