Glutathione S-transferase
From Proteopedia
(Difference between revisions)
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**[[1v40]], [[2cvd]], [[3ee2]], [[3kxo]] - hGST + GSH + inhibitor<br /> | **[[1v40]], [[2cvd]], [[3ee2]], [[3kxo]] - hGST + GSH + inhibitor<br /> | ||
**[[3vi5]], [[3vi7]] - hGST (mutant) + GSH + inhibitor<br /> | **[[3vi5]], [[3vi7]] - hGST (mutant) + GSH + inhibitor<br /> | ||
| + | **[[4imn]] – hGST + PEG<br /> | ||
| + | **[[4imo]] – hGST + substrate analog<br /> | ||
**[[2caq]] - ShGST (mutant) + GSH<BR /> | **[[2caq]] - ShGST (mutant) + GSH<BR /> | ||
**[[1pd2]] - rGST + GSH<BR /> | **[[1pd2]] - rGST + GSH<BR /> | ||
Revision as of 10:02, 20 May 2015
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.
3D structures of glutathione S-transferase
Updated on 20-May-2015
