Glutathione and Sulfur Amino Acids in Human Health and Disease 2008
DOI: 10.1002/9780470475973.ch7
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Glutaredoxin and Thioredoxin Enzyme Systems: Catalytic Mechanisms and Physiological Functions

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Cited by 4 publications
(5 citation statements)
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“…The greatest impact of such reactivity would be realized if the homeostatic enzymes themselves (Scheme ) were modified by l -DOPA byproducts. The two principal enzyme systems that mediate sulfhydryl homeostasis within cells are thioredoxin (Trx) and glutaredoxin (Grx), which catalyze the reduction of oxidized cysteine moieties . Thioredoxin effectively reduces intramolecular and intermolecular disulfides as well as sulfenic acids .…”
Section: Resultsmentioning
confidence: 99%
“…The greatest impact of such reactivity would be realized if the homeostatic enzymes themselves (Scheme ) were modified by l -DOPA byproducts. The two principal enzyme systems that mediate sulfhydryl homeostasis within cells are thioredoxin (Trx) and glutaredoxin (Grx), which catalyze the reduction of oxidized cysteine moieties . Thioredoxin effectively reduces intramolecular and intermolecular disulfides as well as sulfenic acids .…”
Section: Resultsmentioning
confidence: 99%
“…The Trx and Grx systems are the two most versatile systems for facilitating peroxide detoxification and disulfide reduction in cells [for reviews see Refs. (109,146,225)]. The Grx system is comprised of NADPH, glutathione reductase, Grx1, and GSH, a cysteine-containing tripeptide that supplies the reducing equivalent to Grx1 allowing it to reduce protein disulfides.…”
Section: A Trx Regulation Of Cellular Redox Balancementioning
confidence: 99%
“…They are also antioxidant proteins that can neutralize cellular oxidants by supplying the reducing equivalents derived from NADPH to peroxidases (79,146,155). Although there is a large degree of overlap among proteins whose cysteines are reduced by the Trx or Grx systems, there is evidence that some target sites are more effectively reduced by one system (225,262), suggesting that under in vivo conditions, a selective mechanism operates for the removal of disulfides and possibly other oxidative PTMs. Trx1 is able to aid the Prx family of peroxidases in the reduction of hydrogen and lipid peroxides (76).…”
Section: A Trx Regulation Of Cellular Redox Balancementioning
confidence: 99%
“…The reduced Trx-(SH)2 may then directly reduce the disulfide in the substrate proteins [40]. Encoded by two different genes, cytosolic (TRX1) and mitochondrial (TRX2) isoforms have few distinctions [41]. While TRX1 and TRX2 are widely expressed in rat brain, TXR1 specifically shows a high expression level in regions of high metabolic activity and oxidative burden (e.g., substantia nigra and subthalamic nucleus) [42, 43].…”
Section: Introductionmentioning
confidence: 99%