YDR513W
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| Systematic name | YDR513W |
| Gene name | GRX2 |
| Aliases | TTR1 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:1471017..1471448 |
| Primary SGDID | S000002921 |
Description of YDR513W: Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has a paralog, GRX1, that arose from the whole genome duplication[1][2][3][4][5][6][7]
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References
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- ↑ Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
- ↑ Collinson EJ, et al. (2002) The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem 277(19):16712-7 SGD PMID 11875065
- ↑ Draculic T, et al. (2000) A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol Microbiol 36(5):1167-74 SGD PMID 10844700
- ↑ Gan ZR, et al. (1990) Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Biochem Biophys Res Commun 168(3):944-51 SGD PMID 2189409
- ↑ Grant CM, et al. (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1490(1-2):33-42 SGD PMID 10786615
- ↑ Luikenhuis S, et al. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell 9(5):1081-91 SGD PMID 9571241
- ↑ Rodriguez-Manzaneque MT, et al. (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19(12):8180-90 SGD PMID 10567543
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