Structural highlights
Function
GLRX8_YEAST Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.[1] [2]
References
- ↑ Mesecke N, Spang A, Deponte M, Herrmann JM. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mol Biol Cell. 2008 Jun;19(6):2673-80. doi: 10.1091/mbc.E07-09-0896. Epub 2008, Apr 9. PMID:18400945 doi:https://dx.doi.org/10.1091/mbc.E07-09-0896
- ↑ Eckers E, Bien M, Stroobant V, Herrmann JM, Deponte M. Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry. 2009 Feb 17;48(6):1410-23. doi: 10.1021/bi801859b. PMID:19166312 doi:https://dx.doi.org/10.1021/bi801859b
