Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.
Ji
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Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
Armstrong
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Gilliland
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GL
D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D005982:Glutathione Transferase / Q000378:metabolism* / Q000648:ultrastructure; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D005982:Glutathione Transferase