Glutathione synthase catalyzes the chemical reaction
ATP + gamma-L-glutamyl-L-cysteine + glycine  ADP + phosphate + glutathione
The 3 substrates of this enzyme are ATP, gamma-L-glutamyl-L-cysteine, and glycine, whereas its 3 products are ADP, phosphate, and glutathione.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).
 The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming).
Other names in common use include glutathione synthetase, and GSH synthetase.
 This enzyme participates in glutamate metabolism and glutathione metabolism.
 At least one compound, Phosphinate is known to inhibit this enzyme.

The biosynthetic mechanisms for synthetases use energy from nucleoside triphosphates, whereas synthases do not.
Glutathione synthetase stays true to this rule, in that it uses the energy generated by ATP.
Initially, the carboxylate group on γ-glutamylcysteine is converted into an acyl phosphate by the transfer of an inorganic phosphate group of ATP to generate an acyl phosphate intermediate.
Then the amino group of glycine participates in a nucleophilic attack, displacing the phosphate group and forming GSH.
After the final GSH product is made, it can be used by glutathione peroxidase to neutralize reactive oxygen species (ROS) such as H₂O₂ or Glutathione S-transferases in the detoxification of xenobiotics.
Glutathione synthase catalyzes the chemical reaction
ATP + gamma-L-glutamyl-L-cysteine + glycine  ADP + phosphate + glutathione
The 3 substrates of this enzyme are ATP, gamma-L-glutamyl-L-cysteine, and glycine, whereas its 3 products are ADP, phosphate, and glutathione.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases).  The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming). Other names in common use include glutathione synthetase, and GSH synthetase.  This enzyme participates in glutamate metabolism and glutathione metabolism.  At least one compound, Phosphinate is known to inhibit this enzyme.
The biosynthetic mechanisms for synthetases use energy from nucleoside triphosphates, whereas synthases do not. Glutathione synthetase stays true to this rule, in that it uses the energy generated by ATP. Initially, the carboxylate group on γ-glutamylcysteine is converted into an acyl phosphate by the transfer of an inorganic phosphate group of ATP to generate an acyl phosphate intermediate. Then the amino group of glycine participates in a nucleophilic attack, displacing the phosphate group and forming GSH. After the final GSH product is made, it can be used by glutathione peroxidase to neutralize reactive oxygen species (ROS) such as H₂O₂ or Glutathione S-transferases in the detoxification of xenobiotics.
Glutathione synthetase