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coli GCL also functions as a monomeric protein (Hibi et al., Biochemical studies of the GCL from plants revealed that these proteins are regulated by redox environment through a mechanism that differs from the heterodimeric enzymes (Jez et al., Arabidopsis GCL showed that the enzyme was inactivated by buthionine sulfoximine, a potent inhibitor of mammalian GCL, and used a random ter-reactant kinetic mechanism with a preferred order of binding for catalysis (Jez et al., 2+ , orients the glutamate γ-carboxylate for attack on the γ-phosphate of ATP, which is positioned by a second Mg 2+ and an active site lysine

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