Function
Thioredoxin (Trx) is an enzyme which facilitates, in its reduced form, the reduction of proteins by cysteine thiol-disulfide exchange[1]. They contain a CXXC motif.
- Trx-1 is a mammalian cellular protein.
- Trx-2 is mitochondria-specific.
- Trx C,M,X,Y are found in prokaryotes.
- Trx F,H,O are found in eukaryotes.
Relevance
Serum Trx level is a predictor of steatohepatitis[2].
Disease
Trx is involved in a wide range of human diseases and conditions including cancer, viral diseases, aging, cardiac conditions and more[3].
Structural highlights
The active site motif Cys-Gly-Pro-Cys is involved in the reduction of disulfide bonds in proteins[4]
3D Structures of Thioredoxin
Thioredoxin 3D structures
- ↑ Gleason FK, Holmgren A. Thioredoxin and related proteins in procaryotes. FEMS Microbiol Rev. 1988 Dec;4(4):271-97. PMID:3152490
- ↑ Sumida Y, Nakashima T, Yoh T, Furutani M, Hirohama A, Kakisaka Y, Nakajima Y, Ishikawa H, Mitsuyoshi H, Okanoue T, Kashima K, Nakamura H, Yodoi J. Serum thioredoxin levels as a predictor of steatohepatitis in patients with nonalcoholic fatty liver disease. J Hepatol. 2003 Jan;38(1):32-8. PMID:12480557
- ↑ Burke-Gaffney A, Callister ME, Nakamura H. Thioredoxin: friend or foe in human disease? Trends Pharmacol Sci. 2005 Aug;26(8):398-404. PMID:15990177 doi:https://dx.doi.org/10.1016/j.tips.2005.06.005
- ↑ Weichsel A, Gasdaska JR, Powis G, Montfort WR. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure. 1996 Jun 15;4(6):735-51. PMID:8805557
