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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Jan;87(1):31–35. doi: 10.1073/pnas.87.1.31

Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III.

Y P Toung 1, T S Hsieh 1, C P Tu 1
PMCID: PMC53193  PMID: 2296588

Abstract

We have characterized a Drosophila glutathione S-transferase (RX:glutathione R-transferase, EC 2.5.1.18) cDNA encoding a protein of 209 amino acids. The cDNA was expressed in Escherichia coli harboring the expression plasmid construct pGTDml-KK. The active enzyme, designated as Drosophila glutathione S-transferase 1-1, had a specific activity toward 1-chloro-2,4-dinitrobenzene comparable to that for the mammalian glutathione S-transferases but did not have as broad a substrate specificity pattern. There is a region of 44 amino acids in this enzyme that shares 66% identity with an analogous region of maize glutathione S-transferase III. Drosophila glutathione S-transferase 1-1 had no obvious homology to any mammalian or parasitic glutathione S-transferases. The gene was found to be a member of a multigene family.

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Selected References

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