Target type: biologicalprocess
The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. [GOC:ai, ISBN:0198506732]
Glutathione catabolic process is a fundamental metabolic pathway responsible for the breakdown and removal of glutathione (GSH), a tripeptide antioxidant playing a crucial role in protecting cells from oxidative stress. The process involves a series of enzymatic reactions that convert GSH into its constituent amino acids: glycine, glutamate, and cysteine.
The initial step in glutathione catabolism is catalyzed by the enzyme gamma-glutamyltransferase (GGT), which cleaves the gamma-glutamyl bond between glutamate and cysteine in GSH. This reaction releases glutamate and produces a cysteinylglycine intermediate.
Next, the enzyme dipeptidase, also known as cysteinylglycine dipeptidase, hydrolyzes the peptide bond between cysteine and glycine in the cysteinylglycine intermediate. This releases cysteine and glycine.
The breakdown of glutathione is tightly regulated, ensuring a balance between GSH synthesis and degradation to maintain appropriate levels of the antioxidant. Various factors can influence glutathione catabolism, including the presence of reactive oxygen species (ROS), the level of cellular stress, and the activity of enzymes involved in the pathway.
The products of glutathione catabolism, namely glutamate, cysteine, and glycine, can be recycled for biosynthesis or further metabolism. Cysteine is a key precursor for the synthesis of glutathione itself, highlighting the cyclical nature of this process.
Defects in glutathione catabolism can lead to a buildup of GSH, potentially causing toxicity. Conversely, a reduction in glutathione catabolic activity can lead to decreased antioxidant capacity and increased susceptibility to oxidative stress. Therefore, maintaining a balanced glutathione catabolic process is critical for cellular health and homeostasis.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Glutathione hydrolase 1 proenzyme | A glutathione hydrolase 1 proenzyme that is encoded in the genome of human. [PRO:CNA, UniProtKB:P19440] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| aspirin | acetylsalicylate : A benzoate that is the conjugate base of acetylsalicylic acid, arising from deprotonation of the carboxy group. acetylsalicylic acid : A member of the class of benzoic acids that is salicylic acid in which the hydrogen that is attached to the phenolic hydroxy group has been replaced by an acetoxy group. A non-steroidal anti-inflammatory drug with cyclooxygenase inhibitor activity. Aspirin: The prototypical analgesic used in the treatment of mild to moderate pain. It has anti-inflammatory and antipyretic properties and acts as an inhibitor of cyclooxygenase which results in the inhibition of the biosynthesis of prostaglandins. Aspirin also inhibits platelet aggregation and is used in the prevention of arterial and venous thrombosis. (From Martindale, The Extra Pharmacopoeia, 30th ed, p5) | benzoic acids; phenyl acetates; salicylates | anticoagulant; antipyretic; cyclooxygenase 1 inhibitor; cyclooxygenase 2 inhibitor; drug allergen; EC 1.1.1.188 (prostaglandin-F synthase) inhibitor; geroprotector; non-narcotic analgesic; non-steroidal anti-inflammatory drug; plant activator; platelet aggregation inhibitor; prostaglandin antagonist; teratogenic agent |