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F r o m W i k i p e d i a , t h e f r e e e n c y c l o p e d i a
Ubiquitous antioxidant compound in living organisms
Glutathione[1]
Names
IUPAC name
γ-Glutamylcysteinylglycine
Systematic IUPAC name
(2 S 2 R
Other names
γ-L L 2 S 1 R
Identifiers
CAS Number
3D model (JSmol )
Abbreviations
GSH
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.000.660
IUPHAR/BPS
KEGG
MeSH
Glutathione
PubChem CID
UNII
CompTox Dashboard (EPA )
InChI=1S/C10H17N3O6S/c11-5(10(18 )19)1-2-7(14 )13-6(4-20)9(17 )12-3-8(15 )16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1 Y
Key: RWSXRVCMGQZWBV-WDSKDSINSA-N Y
C(CC(=O)N[C@@H](CS )C(=O)NCC(=O)O)[C@@H](C(=O)O)N
Properties
Chemical formula
C 10 H 17 N 3 O 6 S
Molar mass
−1
Melting point
195 °C (383 °F; 468 K )[1]
Solubility in water
Freely soluble[1]
Solubility in methanol , diethyl ether
Insoluble[1]
Pharmacology
ATC code
V03AB32 (WHO
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references
Chemical compound
Glutathione (GSH , ) is an organic compound with the chemical formula HOCOCH(NH 2 2 CH 2 CH 2 SH )CONHCH2 . It is an antioxidant in plants , animals , fungi , and some bacteria and archaea . Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species , free radicals , peroxides , lipid peroxides , and heavy metals .[2] tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine . The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine .
Biosynthesis and occurrence [ edit ]
Glutathione biosynthesis involves two adenosine triphosphate -dependent steps:
While all animal cells are capable of synthesizing glutathione, glutathione synthesis in the liver has been shown to be essential. GCLC knockout mice die within a month of birth due to the absence of hepatic GSH synthesis.[4] [5]
The unusual gamma amide linkage in glutathione protects it from hydrolysis by peptidases.[6]
Occurrence [ edit ]
Glutathione is the most abundant non-protein thiol (R−SH -containing compound) in animal cells, ranging from 0.5 to 10 mmol/L. It is present in the cytosol and the organelles .[6] [7] mitochondria .[8]
Human beings synthesize glutathione, but a few eukaryotes do not, including some members of Fabaceae , Entamoeba Giardia archaea that make glutathione are halobacteria . Some bacteria , such as "Cyanobacteria " and Pseudomonadota , can biosynthesize glutathione.[9] [10]
Systemic availability of orally consumed glutathione has poor bioavailability because the tripeptide is the substrate of proteases (peptidases) of the alimentary canal , and due to the absence of a specific carrier of glutathione at the level of cell membrane.[11] [12] [13] [14] [15]
Biochemical function [ edit ]
Glutathione exists in reduced (GSH) and oxidized (GSSG ) states.[16] oxidative stress [17] [8]
In the reduced state, the thiol group of cysteinyl residue is a source of one reducing equivalent . Glutathione disulfide (GSSG) is thereby generated. The oxidized state is converted to the reduced state by NADPH .[18] glutathione reductase :
NADPH + GSSG + H2 + + OH−
Antioxidant [ edit ]
GSH protects cells by neutralising (reducing) reactive oxygen species .[19] [6]
2 GSH + R2 O 2 (R = H, alkyl)
and with free radicals:
GSH + R• → 1 / 2
Regulation [ edit ]
Aside from deactivating radicals and reactive oxidants, glutathione participates in thiol protection and redox regulation of cellular thiol proteins under oxidative stress by protein S [20]
RSH + GSH + [O ] → GSSR + H2 O
Glutathione is also employed for the detoxification of methylglyoxal and formaldehyde , toxic metabolites produced under oxidative stress. This detoxification reaction is carried out by the glyoxalase system . Glyoxalase I (EC 4.4.1.5) catalyzes the conversion of methylglyoxal and reduced glutathione to S D Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S D D
It maintains exogenous antioxidants such as vitamins C and E [21] [22] [23]
Metabolism [ edit ]
Among the many metabolic processes in which it participates, glutathione is required for the biosynthesis of leukotrienes and prostaglandins . It plays a role in the storage of cysteine. Glutathione enhances the function of citrulline as part of the nitric oxide cycle.[24] cofactor and acts on glutathione peroxidase .[25] hydrogen sulfide metabolism.[26]
Conjugation [ edit ]
Glutathione facilitates metabolism of xenobiotics . Glutathione S enzymes catalyze its conjugation to lipophilic xenobiotics, facilitating their excretion or further metabolism.[27] N p metabolite formed by the action of cytochrome P450 on paracetamol (acetaminophen). Glutathione conjugates to NAPQI, and the resulting ensemble is excreted.
In plants [ edit ]
In plants, glutathione is involved in stress management. It is a component of the glutathione-ascorbate cycle , a system that reduces poisonous hydrogen peroxide .[28] phytochelatins , glutathione oligomers that chelate heavy metals such as cadmium .[29] Pseudomonas syringae Phytophthora brassicae[30] Adenylyl-sulfate reductase , an enzyme of the sulfur assimilation pathway, uses glutathione as an electron donor. Other enzymes using glutathione as a substrate are glutaredoxins . These small oxidoreductases are involved in flower development, salicylic acid , and plant defence signalling.[31]
Winemaking [ edit ]
The content of glutathione in must , the first raw form of wine, determines the browning , or caramelizing effect, during the production of white wine by trapping the caffeoyltartaric acid quinones generated by enzymic oxidation as grape reaction product .[32] [33]
See also [ edit ]
References [ edit ]
^ Pompella A, Visvikis A, Paolicchi A, De Tata V, Casini AF (October 2003). "The changing faces of glutathione, a cellular protagonist". Biochemical Pharmacology . 66 8 ): 1499–1503. doi :10.1016/S0006-2952(03 )00504-5 . PMID 14555227 .
^ White CC, Viernes H, Krejsa CM, Botta D, Kavanagh TJ (July 2003). "Fluorescence-based microtiter plate assay for glutamate-cysteine ligase activity" . Analytical Biochemistry . 318 (2 ): 175–180. doi :10.1016/S0003-2697(03 )00143-X . PMID 12814619 .
^ Chen Y, Yang Y, Miller ML, Shen D, Shertzer HG, Stringer KF, Wang B, Schneider SN, Nebert DW, Dalton TP (May 2007). "Hepatocyte-specific Gclc deletion leads to rapid onset of steatosis with mitochondrial injury and liver failure" . Hepatology . 45 5 ): 1118–1128. doi :10.1002/hep.21635 PMID 17464988 . S2CID 25000753 .
^ Sies H (1999). "Glutathione and its role in cellular functions". Free Radical Biology & Medicine . 27 doi :10.1016/S0891-5849(99 )00177-X . PMID 10569624 .
^ a b c Guoyao Wu; Yun-Zhong Fang; Sheng Yang; Joanne R. Lupton; Nancy D. Turner (2004). "Glutathione Metabolism and its Implications for Health" . Journal of Nutrition . 134 (3 ): 489–492. doi :10.1093/jn/134.3.489 PMID 14988435 .
^ Halprin KM, Ohkawara A (1967). "The measurement of glutathione in human epidermis using glutathione reductase" . The Journal of Investigative Dermatology . 48 2 ): 149–152. doi :10.1038/jid.1967.24 PMID 6020678 .
^ a b Lu SC (May 2013). "Glutathione synthesis" . Biochimica et Biophysica Acta (BBA) - General Subjects . 1830 (5 ): 3143–3153. doi :10.1016/j.bbagen.2012.09.008 . PMC 3549305 PMID 22995213 .
^ Copley SD, Dhillon JK (29 April 2002). "Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes" . Genome Biology . 3 5 ): research0025. doi :10.1186/gb-2002-3-5-research0025 PMC 115227 PMID 12049666 .
^ Wonisch W, Schaur RJ (2001). "Chapter 2: Chemistry of Glutathione" . In Grill D, Tausz T, De Kok L (eds.). Significance of glutathione in plant adaptation to the environment ISBN 978-1-4020-0178-9
^ Witschi A, Reddy S, Stofer B, Lauterburg BH (1992). "The systemic availability of oral glutathione". European Journal of Clinical Pharmacology . 43 6 ): 667–669. doi :10.1007/bf02284971 . PMID 1362956 . S2CID 27606314 .
^ "Acetylcysteine Monograph for Professionals" . Drugs.com .
^ Atkuri, K. R.; Mantovani, J. J.; Herzenberg, L. A.; Herzenberg, L. A. (2007). "N-acetylcysteine - a safe antidote for cysteine/glutathione deficiency" . Current Opinion in Pharmacology . 7 4 ): 355–359. doi :10.1016/j.coph.2007.04.005 . PMC 4540061 PMID 17602868 .
^ Nagasawa, Herbert T. (27 November 2014). "COMPOSITIONS COMPRISING SUGAR-CYSTEINE PRODUCTS - US-20140348811-A1" . ppubs.uspto.gov . United States Patent Office. p. 16 . Retrieved 31 October 2023 . 30. A method of increasing ATP and/or glutathione...
^ Ukwenya VO, Alese MO, Ogunlade B, Folorunso IM, Omotuyi OI (2022). "Anacardium occidentale leaves extract and riboceine mitigate hyperglycemia through anti-oxidative effects and modulation of some selected genes associated with diabetes" . J Diabetes Metab Disord . 22 1 ): 455–468. doi :10.1007/s40200-022-01165-2 . PMC 10225389 PMID 37255827 .
^ Iskusnykh IY, Zakharova AA, Pathak D (January 2022). "Glutathione in Brain Disorders and Aging" . Molecules . 27 1 ): 324. doi :10.3390/molecules27010324 PMC 8746815 PMID 35011559 .
^ Pastore A, Piemonte F, Locatelli M, Lo Russo A, Gaeta LM, Tozzi G, Federici G (August 2001). "Determination of blood total, reduced, and oxidized glutathione in pediatric subjects" . Clinical Chemistry . 47 8 ): 1467–1469. doi :10.1093/clinchem/47.8.1467 PMID 11468240 .
^ Couto N, Malys N, Gaskell SJ, Barber J (June 2013). "Partition and turnover of glutathione reductase from Saccharomyces cerevisiae: a proteomic approach" (PDF) . Journal of Proteome Research . 12 6 ): 2885–2894. doi :10.1021/pr4001948 . PMID 23631642 .
^ Michael Brownlee (2005). "The pathobiology of diabetic complications: A unifying mechanism" . Diabetes . 54 6 ): 1615–1625. doi :10.2337/diabetes.54.6.1615 PMID 15919781 .
^ Dalle-Donne, Isabella; Rossi, Ranieri; Colombo, Graziano; Giustarini, Daniela; Milzani, Aldo (2009). "Protein S Trends in Biochemical Sciences . 34 2 ): 85–96. doi :10.1016/j.tibs.2008.11.002 . PMID 19135374 .
^ Dringen R (December 2000). "Metabolism and functions of glutathione in brain". Progress in Neurobiology . 62 6 ): 649–671. doi :10.1016/s0301-0082(99 )00060-x . PMID 10880854 . S2CID 452394 .
^ Scholz RW, Graham KS, Gumpricht E, Reddy CC (1989). "Mechanism of interaction of vitamin E and glutathione in the protection against membrane lipid peroxidation". Annals of the New York Academy of Sciences . 570 (1 ): 514–517. Bibcode :1989NYASA.570..514S . doi :10.1111/j.1749-6632.1989.tb14973.x . S2CID 85414084 .
^ Hughes RE (1964). "Reduction of dehydroascorbic acid by animal tissues". Nature . 203 (4949): 1068–1069. Bibcode :1964Natur.203.1068H . doi :10.1038/2031068a0 . PMID 14223080 . S2CID 4273230 .
^ Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS (June 1999). "Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe " . The Plant Cell . 11 6 ): 1153–1164. doi :10.1105/tpc.11.6.1153 . JSTOR 3870806 . PMC 144235 PMID 10368185 .
^ Grant CM (2001). "Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions" . Molecular Microbiology . 39 3 ): 533–541. doi :10.1046/j.1365-2958.2001.02283.x PMID 11169096 . S2CID 6467802 .
^ Melideo, SL; Jackson, MR; Jorns, MS (22 July 2014). "Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog" . Biochemistry . 53 28 ): 4739–53. doi :10.1021/bi500650h . PMC 4108183 PMID 24981631 .
^ Hayes, John D.; Flanagan, Jack U.; Jowsey, Ian R. (2005). "Glutathione transferases". Annual Review of Pharmacology and Toxicology . 45 doi :10.1146/annurev.pharmtox.45.120403.095857 . PMID 15822171 .
^ Noctor G, Foyer CH (June 1998). "Ascorbate and Glutathione: Keeping Active Oxygen Under Control". Annual Review of Plant Physiology and Plant Molecular Biology . 49 1 ): 249–279. doi :10.1146/annurev.arplant.49.1.249 . PMID 15012235 .
^ Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS (June 1999). "Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe" . The Plant Cell . 11 6 ): 1153–1164. doi :10.1105/tpc.11.6.1153 . PMC 144235 PMID 10368185 .
^ Parisy V, Poinssot B, Owsianowski L, Buchala A, Glazebrook J, Mauch F (January 2007). "Identification of PAD2 as a gamma-glutamylcysteine synthetase highlights the importance of glutathione in disease resistance of Arabidopsis" (PDF) . The Plant Journal . 49 1 ): 159–172. doi :10.1111/j.1365-313X.2006.02938.x PMID 17144898 .
^ Rouhier N, Lemaire SD, Jacquot JP (2008). "The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation" (PDF) . Annual Review of Plant Biology . 59 1 ): 143–166. doi :10.1146/annurev.arplant.59.032607.092811 . PMID 18444899 .
^ Rigaud J, Cheynier V, Souquet JM, Moutounet M (1991). "Influence of must composition on phenolic oxidation kinetics" . Journal of the Science of Food and Agriculture . 57 1 ): 55–63. Bibcode :1991JSFA...57...55R . doi :10.1002/jsfa.2740570107 .
^ Vallverdú-Queralt A, Verbaere A, Meudec E, Cheynier V, Sommerer N (January 2015). "Straightforward method to quantify GSH, GSSG, GRP, and hydroxycinnamic acids in wines by UPLC-MRM-MS". Journal of Agricultural and Food Chemistry . 63 1 ): 142–149. doi :10.1021/jf504383g . PMID 25457918 .
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AMPAR Tooltip α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor
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R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Glutathione&oldid=1226591470 " C a t e g o r i e s : ● T h i o l s ● T r i p e p t i d e s ● A n t i o x i d a n t s H i d d e n c a t e g o r i e s : ● A r t i c l e s w i t h s h o r t d e s c r i p t i o n ● S h o r t d e s c r i p t i o n m a t c h e s W i k i d a t a ● U s e d m y d a t e s f r o m A u g u s t 2 0 2 1 ● A r t i c l e s w i t h o u t I n C h I s o u r c e ● E C H A I n f o C a r d I D f r o m W i k i d a t a ● A r t i c l e s c o n t a i n i n g u n v e r i f i e d c h e m i c a l i n f o b o x e s ● S h o r t d e s c r i p t i o n i s d i f f e r e n t f r o m W i k i d a t a ● A r t i c l e s w i t h B N F i d e n t i f i e r s ● A r t i c l e s w i t h B N F d a t a i d e n t i f i e r s ● A r t i c l e s w i t h J 9 U i d e n t i f i e r s ● A r t i c l e s w i t h L C C N i d e n t i f i e r s ● A r t i c l e s w i t h N D L i d e n t i f i e r s
● T h i s p a g e w a s l a s t e d i t e d o n 3 1 M a y 2 0 2 4 , a t 1 6 : 4 1 ( U T C ) . ● T e x t i s a v a i l a b l e u n d e r t h e C r e a t i v e C o m m o n s A t t r i b u t i o n - S h a r e A l i k e L i c e n s e 4 . 0 ;
a d d i t i o n a l t e r m s m a y a p p l y . B y u s i n g t h i s s i t e , y o u a g r e e t o t h e T e r m s o f U s e a n d P r i v a c y P o l i c y . W i k i p e d i a ® i s a r e g i s t e r e d t r a d e m a r k o f t h e W i k i m e d i a F o u n d a t i o n , I n c . , a n o n - p r o f i t o r g a n i z a t i o n . ● P r i v a c y p o l i c y ● A b o u t W i k i p e d i a ● D i s c l a i m e r s ● C o n t a c t W i k i p e d i a ● C o d e o f C o n d u c t ● D e v e l o p e r s ● S t a t i s t i c s ● C o o k i e s t a t e m e n t ● M o b i l e v i e w ●
T o g g l e l i m i t e d c o n t e n t w i d t h
