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It is known that, in rat and human GLCL holoenzyme, cystamine completely inactivates rat GLCL activity by interaction with a thiol group that is thought to be at or near the l-glutamate-binding site in the wild enzyme [135,136,137,138] and also in a recombinant mutant (hGLCLC-C553G) where one cysteine group far from the active site was selectively inactivated [139]