Rational reconstruction of the active site of a class mu glutathione S-transferase.

@article{Shan1994RationalRO,
  title={Rational reconstruction of the active site of a class mu glutathione S-transferase.},
  author={Siqing Shan and Richard N. Armstrong},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 51},
  pages={32373-9}
}
Isoenzymes 3-3 and 4-4 of the mu class glutathione S-transferases share 77% sequence identity but have distinctly different catalytic properties. Analysis of the crystal structure of isoenzyme 3-3 in complex with the diastereomeric products of the addition of GSH to phenanthrene 9,10-oxide (Ji, X., Johnson, W. W., Sesay, M. A., Dickert, L., Prasad, S. M., Ammon, H. L., Armstrong, R. N., and Gilliland, G. L. (1994) Biochemistry 33, 1043-1052) reveals that 3 residues that are in van der Waals… CONTINUE READING

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