Glutathione S-transferase
From Proteopedia
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== 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>. | ||
| - | * | + | *'''epsilon glutathione S-transferase''' has a role in insecticide resistance<ref>PMID:26487708</ref>. |
==Relevance== | ==Relevance== | ||
Revision as of 10:30, 25 June 2024
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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
- ↑ Wongsantichon J, Robinson RC, Ketterman AJ. Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. Biosci Rep. 2015 Oct 20;35(6). pii: e00272. doi: 10.1042/BSR20150183. PMID:26487708 doi:http://dx.doi.org/10.1042/BSR20150183
- ↑ 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
