Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu.

Glutathione S-transferases constitute a family of enzymes that detoxify xenobiotics by conjugating glutathione with a range of electrophilic substrates. The cytosolic glutathione S-transferase dimeric isoenzymes are currently divided into at least eight classes on the basis of their physical and chemical properties. Previously, heterodimers have only been detected within a given class of isoenzymes; however, here we describe for the first time the generation of a heterodimer between a pi class and mu class glutathione S-transferase. The heterodimer forms under mild conditions (dialysis against phosphate buffer, pH 6.5) and is best detected when one of the isoenzyme subunits is in excess. The activity of the pi-mu heterodimer toward several substrates indicates that interaction between these two dissimilar subunits influences the catalytic activity of this dimer. The production of this new heterodimer provides a new approach in glutathione S-transferase research to study the influence of one subunit on the catalytic activity of its partner subunit and to identify those amino acid residues which contribute to subunit interactions.