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    Biochem J. 1997 Dec 15;328 ( Pt 3):929-35.

    Zeta, a novel class of glutathione transferases in a range of species from plants to humans.

    Board PG, Baker RT, Chelvanayagam G, Jermiin LS.

    Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, GPO Box 34, Canberra, ACT 2601, Australia.

    Sequence alignment and phylogenetic analysis has identified a new subgroup of glutathione S-transferase (GST)-like proteins from a range of species extending from plants to humans. This group has been termed the Zeta class. An atomic model of the N-terminal domain suggests that the members of the Zeta class have a similar structure to that of other GSTs, binding glutathione in a similar orientation in the G site. Recombinant human GSTZ1-1 has been expressed in Escherichia coli and characterized. The protein is a dimer composed of 24.2 kDa subunits and has minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole. Although low in comparison with other GSTs, GSTZ1-1 has glutathione peroxidase activity with t-butyl and cumene hydroperoxides. The members of the Zeta class have been conserved over a long evolutionary period, suggesting that they might have a role in the metabolism of a compound that is common in many living cells.

    PMID: 9396740 [PubMed - indexed for MEDLINE]

    PMCID: PMC1219006

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