Structural highlights
Function
[GLRX1_YEAST] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Luikenhuis S, Perrone G, Dawes IW, Grant CM. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell. 1998 May;9(5):1081-91. PMID:9571241
- ↑ Collinson EJ, Wheeler GL, Garrido EO, Avery AM, Avery SV, Grant CM. The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem. 2002 May 10;277(19):16712-7. Epub 2002 Mar 1. PMID:11875065 doi:http://dx.doi.org/10.1074/jbc.M111686200
- ↑ Collinson EJ, Grant CM. Role of yeast glutaredoxins as glutathione S-transferases. J Biol Chem. 2003 Jun 20;278(25):22492-7. Epub 2003 Apr 8. PMID:12684511 doi:http://dx.doi.org/10.1074/jbc.M301387200
