Article
Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione transferase P1-1.
Biochimica et biophysica acta - 26 Jun 2003
Lin Henry J, Johansson Ann Sofie, Stenberg Gun, Materi Alicia M, Park Jae Man, Dai Aihua, Zhou Haiyan, Gim Jason S Y, Kau Irving H, Hardy Steven I, Parker Michael W, Mannervik Bengt
Abstract excerpt
Glutathione transferases (GSTs) are a family of enzymes that detoxify electrophilic compounds, such as carcinogens or drugs, by conjugating them to glutathione. The enzymes have contributed to the understanding of protein structure, due to large differences in amino acid sequence within the family, yet similar architecture and folding. Our objective was to conduct a systematic survey of GSTP1 polymorphisms and...
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