Glutathione S-transferase

Function

Glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione (GSH) to a variety of exogenous and endogenous hydrophobic electrophiles. For example, GST can detoxify peroxidised lipids. All eukaryotes possess a variety of GSTs with catalytic and non-catalytic activities. GST is divided into classes: α, δ, ε, κ, μ, ν, ω, π, ρ, σ (hematopoietic prostaglandin D synthase), τ, χ, ϑ, ζ and microsomal^[1].

Relevance

GST are targets for anti-diabetic drugs.

Structural highlights

The glutathione binding site is at the N-terminal of GST^[2].

3D structures of glutathione S-transferase

Updated on 10-March-2016

References

1. ↑ Oakley A. Glutathione transferases: a structural perspective. Drug Metab Rev. 2011 May;43(2):138-51. doi: 10.3109/03602532.2011.558093. Epub, 2011 Mar 23. PMID:21428697 doi:http://dx.doi.org/10.3109/03602532.2011.558093
2. ↑ Rossjohn J, Feil SC, Wilce MC, Sexton JL, Spithill TW, Parker MW. Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase. J Mol Biol. 1997 Nov 7;273(4):857-72. PMID:9367777 doi:10.1006/jmbi.1997.1338