A subgroup of class α glutathione S‐transferases Cloning of cDNA for mouse lung glutathione S‐transferase GST 5.7

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Abstract
A full-length cDNA clone encoding the previously purified mouse glutathione S-transferase GST 5.7 [(1991), Biochem. J. 278, 793–799] has been isolated from a mouse lung cDNA library in λgt11. Sequencing of the clone revealed the presence of microheterogeneity in GST 5.7. Comparison of the deduced protein sequence with other glutathione S-transferases, together with previous information available on GST 5.7, indicates that the enzyme belongs to a novel subgroup within the α class of glutathione S-transferases. Members of the subgroup, which also include the rat GST 8-8 and perhaps chicken GST CL3, show high sequence homology with each other, but only moderate similarity to other α class enzymes. They share a substrate specificity profile that resembles π-class enzymes, and are active in the conjugation of lipid peroxidation products.

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