Glutathione S-transferase
From Proteopedia
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| + | <StructureSection load='1fhe' size='350' side='right' caption='Glutathione S-tansferase complex with glutathione (PDB entry [[1fhe]])' scene=''> | ||
== Function == | == 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<ref>PMID:21428697</ref> . | + | '''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>. |
==Relevance== | ==Relevance== | ||
GST are targets for anti-diabetic drugs. | GST are targets for anti-diabetic drugs. | ||
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| + | == Structural highlights == | ||
| + | The glutathione binding site is at the N-terminal of GST<ref>PMID:9367777</ref>. | ||
==3D structures of glutathione S-transferase== | ==3D structures of glutathione S-transferase== | ||
Revision as of 11:23, 10 March 2016
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