Glutathione transferase omega

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Glutathione transferase omega

Existing structural data : 1eem

Mass / length primary structure 241/243 amino acids
Secondary to quaternary structure Homodimer
Identifier
Gene name (s) GSTO1 , GSTO2
External IDs
Enzyme classification
EC, category 2.5.1.18 transferase
Occurrence
Parent taxon Mammals, insects, worms

Glutathione transferases omega (GSTO) are enzymes in mammals, insects and worms that can reduce dehydroascorbic acid and monomethyl arsenate with the help of glutathione . They therefore play an important role in the recycling of vitamin C and in the biotransformation of arsenic compounds . Two paralogues are known in humans , which are encoded by the genes GSTO1 and GSTO2 . GSTO-1 occurs in the cytoplasm of all tissue types, but especially in the liver , skeletal muscles and in the heart . GSTO-2 is also produced everywhere, but especially in the testes .

The GSTO belong to the group of glutathione-S-transferases and are characterized by the fact that a cysteine residue acts as the catalytic center and by their dehydroascorbate reductase activity.

Other functions of GSTO-1 that have been discovered are modulation of the ryanodine receptor and interaction with drugs that inhibit the release of cytokines .

There may be variants of GSTO-1 associated with amyotrophic lateral sclerosis , others may increase the risk of breast cancer , and others may be associated with cerebral atherosclerosis . GSTO-1 is a possible candidate as the cause of the platinum resistance phenomenon .

Catalyzed reactions

DeAsc+ 2 GSH   + GSSG  Asc

Dehydroascorbic acid is reduced to ascorbic acid, while glutathione is oxidized to glutathione disulfide.

Individual evidence

  1. UniProt P78417
  2. ^ A b c Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG: Characterization of the omega class of glutathione transferases . In: Meth. Enzymol. . 401, 2005, pp. 78-99. doi : 10.1016 / S0076-6879 (05) 01005-0 . PMID 16399380 .
  3. ^ Van de Giessen E, Fogh I, Gopinath S, et al : Association study on glutathione S-transferase omega 1 and 2 and familial ALS . In: Amyotroph Lateral Scler . 9, No. 2, April 2008, pp. 81-4. doi : 10.1080 / 17482960701702553 . PMID 18427999 .
  4. Olsen A, Autrup H, Sørensen M, Overvad K, Tjønneland A: Polymorphisms of glutathione S-transferase A1 and O1 and breast cancer among postmenopausal Danish women . In: Eur J Cancer Prev . 17, No. 3, June 2008, pp. 225-9. doi : 10.1097 / CEJ.0b013e3282b6fe1e . PMID 18414193 .
  5. Kölsch H, Larionov S, Dedeck O, et al : Association of the glutathione S-transferase omega-1 Ala140Asp polymorphism with cerebrovascular atherosclerosis and plaque-associated interleukin-1 alpha expression . In: Stroke . 38, No. 10, October 2007, pp. 2847-50. doi : 10.1161 / STROKEAHA.107.484162 . PMID 17717316 .
  6. Yan XD, Pan LY, Yuan Y, Lang JH, Mao N: Identification of platinum-resistance associated proteins through proteomic analysis of human ovarian cancer cells and their platinum-resistant sublines . In: J. Proteome Res . 6, No. 2, February 2007, pp. 772-80. doi : 10.1021 / pr060402r . PMID 17269733 .
  7. D'Eustachio / reactome.org: Reduction of dehydroascorbate to ascorbate  ( page no longer available , search in web archivesInfo: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice. .@1@ 2Template: Dead Link / www.reactome.org