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“Most glutathione studies that are done used either IV or oral glutathione, and the dose used commonly could be anywhere from 500 milligrams to 2 grams,” explains Dr. Patel.
Glutathione (GSH, / ˌ ɡ l uː t ə ˈ θ aɪ oʊ n /) is an organic compound with the chemical formula HOCOCH(NH 2)CH 2 CH 2 CONHCH(CH 2 SH)CONHCH 2 COOH. It is an antioxidant in plants , animals , fungi , and some bacteria and archaea .
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. [2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants. [3]
The glutathione binding site, or "G-site", is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs. The region containing the greatest amount of variability between the assorted classes is that of helix α2 , where one of three different amino acid residues interacts with the glycine residue of glutathione.
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Glutamate–cysteine ligase (GCL) EC 6.3.2.2), previously known as γ-glutamylcysteine synthetase (GCS), is the first enzyme of the cellular glutathione (GSH) biosynthetic pathway that catalyzes the chemical reaction: L-glutamate + L-cysteine + ATP γ-glutamyl cysteine + ADP + P i
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100042625 Ensembl ENSG00000084207 n/a UniProt P09211 n/a RefSeq (mRNA) NM_000852 XM_036155425 RefSeq (protein) NP_000843 n/a Location (UCSC) Chr 11: 67.58 – 67.59 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene. Function Glutathione S-transferases (GSTs) are a family of enzymes that play an ...