The activities of maize GSTs from the phi and tau classes were examined in
recombinant bacteria expressing heterodimers or chimeric subunits. Heterodi
mer formation was successful between GSTs within a class, but not between G
STs from different classes. The activity and kinetics of heterodimers compa
red with homodimers was additive; the subunit active sites appeared kinetic
ally independent. N-terminal domains were swapped between GSTs to give chim
eras; those formed between GSTs of different classes were inactive. Most in
tra-class chimeras were active and allowed the influence of each of the two
domains on various kinetic properties to be investigated. (C) 2001 Elsevie
r Science Ireland Ltd. All rights reserved.