Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.

@article{Nilsson2000RedesignOS,
  title={Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.},
  author={Lisa O Nilsson and Ann Gustafsson and Bengt Mannervik},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 17},
  pages={9408-12}
}
The evolution of proteins for novel functions involves point mutations and recombinations of domains or structural segments. Mimicking this process by rational design in vitro is still a major challenge. The present report demonstrates that the active site of the enzyme glutathione transferase (GST) A1-1 can be tailored for high catalytic efficiency with alkenals. The result is a >3,000-fold change in substrate selectivity involving a noteworthy change in preferred catalyzed reaction from… CONTINUE READING

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