Glutathione S-transferase
From Proteopedia
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{{STRUCTURE_1pkw| PDB=1pkw | SIZE=400| SCENE= |right|CAPTION=Human glutathione S-transferase α class A1-1 dimer complex with glutathione and hydroxyethyl bisulfide [[1pkw]] }} | {{STRUCTURE_1pkw| PDB=1pkw | SIZE=400| SCENE= |right|CAPTION=Human glutathione S-transferase α class A1-1 dimer complex with glutathione and hydroxyethyl bisulfide [[1pkw]] }} | ||
| - | + | == 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. | + | '''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<ref>PMID:21428697</ref> . |
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| + | ==Relevance== | ||
| + | GST are targets for anti-diabetic drugs. | ||
==3D structures of glutathione S-transferase== | ==3D structures of glutathione S-transferase== | ||
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**[[2h8a]] - rGST + GSH<BR /> | **[[2h8a]] - rGST + GSH<BR /> | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:59, 10 March 2016
Contents |
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.
3D structures of glutathione S-transferase
Updated on 10-March-2016
References
- ↑ 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
