Glutathione S-transferases

 

GST conjugate the tripeptide glutathione to various chemical substrates - often as part of phase II of detoxification. A typical detoxification may involve a P450 adding a hydroxyl group to a substrate (phase I) that then enables a GST to add the glutathione (phase II) which can assist in the excretion of that compound. 

Low, W.Y, Feil, S., Ng, H.L., Gorman, M.A., Morton, C.J., Pyke, J., McConville, M.J., Michael Bieri, Yee-Foong Mok, Robin, C+, Gooley, P.R., Parker, M.W., and Batterham, P. (2010) Structural insights of the binding of glutathione and DDT to Drosophila melanogaster GSTD1. Journal of Molecular Biology. 399(3): 358-366.

Low, W.Y., Ng, H.L., Morton, C.J., Parker, M.W., Batterham, P., Robin, C., (2007) Positive selection of Glutathione S-Transferases in the genus, Drosophila. Genetics.173(3)1363-1375.

Drosophila Comparative Genome Sequencing and Analysis Consortium. (2007) Genomics on a Phylogeny: Evolution of Genes and Genomes in the Genus Drosophila. Nature 450 :203-218.

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The Drosophila enzyme GST D1 showing the insecticide DDT in the active site (white). We confirmed GSTD1 is indeed a DDTase, characterized its crystal structure at high resolution and examined the way the structure changed with addition of DDT using NMR.

Collaborators include Bio21 Institute colleagues:

Michael Parker

Paul Gooley

Malcolm McConville

Phil Batterham