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=''> | + | <StructureSection load='1fhe' size='350' side='right' caption='Glutathione S-tansferase complex with glutathione (PDB entry [[1fhe]])' scene='52/524296/Cv/1'> |
== 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>. | ||
Revision as of 11:57, 16 March 2016
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3D structures of glutathione S-transferase
Updated on 16-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
- ↑ 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
