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Structural and functional characterization of GS from bacteria demonstrates that this enzyme functions as a tetramer (Yamaguchi et al., Arabidopsis , wheat ( Triticum aestivum ), maize ( Zea mays ), and various legumes share ~40% amino acid sequence identity with the human and yeast homologs (Rawlins et al., Early mutagenesis studies of the Arabidopsis GS identified a putative glycine-rich loop as important for activity (Wang and Oliver, Arabidopsis GS uses a random Ter-reactant mechanism with binding of either ATP or -glutamylcysteine preferred first and addition of glycine last (Jez and Cahoon, Arabidopsis GS and for the eukaryotic homologs (Herrera et al., 2+ to ATP and orienting the -phosphate group in the active site

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