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during the stage of glutathione synthesis, ATP …

Prokaryotic glutathione synthetase, ATP-grasp domain; ..

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Glutamine synthetase - Wikipedia

In humans, glutathione synthetase functions in a similar manner. Its product GSH participates in cellular pathways involved in homeostasis and cellular maintenance. For instance, catalyze the oxidation of GSH to (GSSG) by reducing free radicals and reactive oxygen species such as hydrogen peroxide. uses GSH to clean up various metabolites, xenobiotics, and electrophiles to for excretion. Because of its antioxidant role, GSS mostly produce GSH inside the cytoplasm of liver cells and imported to mitochondria where detoxification occurs.]] GSH is also essential for the activation of the immune system to generate robust defense mechanisms against invading pathogens. GSH is capable of preventing infection from the influenza virus.

The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway ..

The biosynthetic mechanisms for use energy from , whereas do not. Glutathione synthetase stays true to this rule, in that it uses the energy generated by ATP. Initially, the group on γ-glutamylcysteine is converted into an 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 to neutralize (ROS) such as H2O2 or in the detoxification of .

Glutathione Metabolism and Its Implications for Health

05/12/2003 · Glutathione Metabolism and Its Implications for Health 1

Human and yeast glutathione synthetases are , meaning they are composed of two identical of itself bound to each other. On the other hand, E. coli glutathione synthetase is a . Nevertheless, they are part of the ATP-grasp , which consists of 21 enzymes that contain an ATP-grasp fold. Each subunit interacts with each other through and interactions and contains two domains. One domain facilitates the ATP-grasp mechanism and the other is the catalytic for . The ATP-grasp fold is conserved within the ATP-grasp superfamily and is characterized by two alpha helices and beta sheets that hold onto the ATP molecule between them. The domain containing the active site exhibits interesting properties of specificity. In contrast to γ-glutamylcysteine synthetase, glutathione synthetase accepts a large variety of glutamyl-modified analogs of γ-glutamylcysteine, but is much more specific for cysteine-modified analogs of γ-glutamylcysteine. Crystalline structures have shown glutathione synthetase bound to GSH, ADP, two ions, and a sulfate ion. Two magnesium ions function to stabilize the acylphosphate intermediate, facilitate binding of ATP, and activate removal of phosphate group from ATP. Sulfate ion serves as a replacement for inorganic phosphate once the acylphosphate intermediate is formed inside the active site.

This entry represents the substrate-binding domain of glutathione synthetase () (GSS), a homodimeric enzyme that catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to phosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis, the first step being catalysed by gamma-glutamylcysteine synthetase []. In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, and increased rate of haemolysis and defective function of the central nervous system. The substrate-binding domain has a 3-layer alpha/beta/alpha structure [].

Glutathione is not built by the normal machinery of protein synthesis

Glutathione Promotes DNA and RNA Synthesis

Glutathione synthetase (GSS) (EC is the second enzyme in the (GSH) biosynthesis pathway. It catalyses the condensation of and , to form glutathione. Glutathione synthetase is also a potent antioxidant. It is found in a large number of species including bacteria, yeast, mammals, and plants.

The Biosynthesis of Glutathione - Glutathione
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    Glutamine synthetase ..

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