Glutaredoxin active site
Short name | GLR_AS |
Description
References
1.The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues. Foloppe N, Nilsson L. Structure 12, 289-300, (2004). View articlePMID: 14962389
2.Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds. Holmgren A. Biochem. Soc. Trans. 16, 95-6, (1988). PMID: 3286320
3.Vaccinia virus encodes a protein with similarity to glutaredoxins. Johnson GP, Goebel SJ, Perkus ME, Davis SW, Winslow JP, Paoletti E. Virology 181, 378-81, (1991). View articlePMID: 1994586
4.Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction. Berardi MJ, Bushweller JH. J. Mol. Biol. 292, 151-61, (1999). View articlePMID: 10493864
5.Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J. Biochemistry 37, 17145-56, (1998). View articlePMID: 9860827
6.Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Fernandes AP, Holmgren A. Antioxid. Redox Signal. 6, 63-74, (2004). View articlePMID: 14713336
7.Thioredoxin and related proteins in procaryotes. Gleason FK, Holmgren A. FEMS Microbiol. Rev. 4, 271-97, (1988). PMID: 3152490
8.Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Shelton MD, Chock PB, Mieyal JJ. Antioxid. Redox Signal. 7, 348-66, (2005). View articlePMID: 15706083
9.Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities. Xiao R, Lundstrom-Ljung J, Holmgren A, Gilbert HF. J. Biol. Chem. 280, 21099-106, (2005). View articlePMID: 15814611
10.Thioredoxin and glutaredoxin systems. Holmgren A. J. Biol. Chem. 264, 13963-6, (1989). View articlePMID: 2668278
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS00195