Target type: molecularfunction
Catalysis of the reaction: glutathione + H2O = L-cysteinylglycine + L-glutamate. [EC:3.4.19.13, GOC:imk]
Glutathione hydrolase activity is a crucial enzymatic function involved in the hydrolysis of glutathione, a tripeptide composed of glycine, cysteine, and glutamic acid. This activity is essential for various biological processes, including detoxification, antioxidant defense, and maintaining cellular redox balance.
Glutathione hydrolase enzymes catalyze the cleavage of the gamma-glutamyl bond in glutathione, producing gamma-glutamate and cysteinylglycine. This reaction is highly specific for glutathione and is not typically observed with other peptides.
The breakdown of glutathione by hydrolases contributes to the regulation of glutathione levels within cells. It is particularly important in the detoxification of xenobiotics and reactive oxygen species (ROS). By reducing glutathione levels, hydrolases can make the glutathione available for conjugation reactions, which involve the attachment of glutathione to toxic compounds, facilitating their excretion from the body.
Furthermore, glutathione hydrolase activity plays a role in the antioxidant defense system. Hydrolysis of glutathione can release cysteine, a precursor for the synthesis of glutathione reductase, an enzyme that reduces oxidized glutathione. This process contributes to the regeneration of the reduced form of glutathione, which is crucial for its antioxidant function.
In addition to detoxification and antioxidant defense, glutathione hydrolase activity is involved in various other cellular processes. It has been implicated in the regulation of immune responses, signal transduction pathways, and cell growth and differentiation.
Overall, glutathione hydrolase activity is a critical enzymatic function that plays a significant role in maintaining cellular homeostasis, detoxification, antioxidant defense, and various other biological processes. Its precise role may vary depending on the specific hydrolase enzyme and the cellular context.'
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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) |
| 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 |