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630370 
Journal Article 
Zeta, a novel class of glutathione transferases in a range of species from plants to humans 
Board, PG; Baker, RT; Chelvanayagam, G; Jermiin, LS 
1997 
Yes 
Biochemical Journal
ISSN: 0264-6021
EISSN: 1470-8728 
328 
Pt. 3 
929-935 
English 
9396740 
WOS:000071213800029 
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. 
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