Structural highlights
Function
YFCG_ECOLI Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.[1] [2]
See Also
References
- ↑ Kanai T, Takahashi K, Inoue H. Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress. J Biochem. 2006 Nov;140(5):703-11. Epub 2006 Oct 3. PMID:17018556 doi:http://dx.doi.org/10.1093/jb/mvj199
- ↑ Wadington MC, Ladner JE, Stourman NV, Harp JM, Armstrong RN. Analysis of the Structure and Function of YfcG from Escherichia coli Reveals an Efficient and Unique Disulfide Bond Reductase. Biochemistry. 2009 Jun 23. PMID:19537707 doi:10.1021/bi9008825
