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2739 109801 Ensembl ENSG00000124767 ENSMUSG00000024026 UniProt Q04760 Q9CPU0 RefSeq (mRNA) NM_006708 NM_001113560 NM_025374 RefSeq (protein) NP_006699 NP_001107032 NP_079650 Location (UCSC) Chr 6: 38.68 – 38.7 Mb Chr 17: 30.8 – 30.85 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Lactoylglutathione lyase in humans is encoded by the GLO1 gene. Structure Several structures of ...
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]
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
Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; [1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).
GSNO, along with glutathione and oxidized glutathione (GSSG), have been found to bind to the glutamate recognition site of the NMDA and AMPA receptors (via their γ-glutamyl moieties), and may be endogenous neuromodulators. [18] [19] At millimolar concentrations, they may also modulate the redox state of the NMDA receptor complex. [19]
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