Functional studies of single-nucleotide polymorphic variants of human glutathione transferase T1-1 involving residues in the dimer interface

► Examined SNPs that alter residues in dimer interface of glutathione transferase GST T1-1. ► Measured enzyme kinetics and thermal denaturation properties of variants. ► T104P, previously reported as inactive, showed detectable activity. ► R76S is active but has reduced thermal stability. ► Individuals carrying these SNPs may have altered responses to toxic substrates of GST T1-1.