Active-site Residues Governing High Steroid Isomerase Activity in Human Glutathione Transferase A3-3

This publication has 30 references indexed in Scilit:

• Selective Catalysis of Elementary Steps by Asp-99 and Tyr-14 of 3-Oxo-Δ⁵-Steroid Isomerase
  Journal of the American Chemical Society, 2001
• The Role of Glutathione in the Isomerization of Δ5-Androstene- 3,17-dione Catalyzed by Human Glutathione Transferase A1-1
  Journal of Biological Chemistry, 2001
• Pressure-dependent ionization of Tyr 9 in glutathione S-transferase A1-1: Contribution of the C-terminal helix to a “soft” active site
  Protein Science, 1997
• Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases
  Chemical Research in Toxicology, 1997
• Rational Modulation of the Catalytic Activity of A1-1 Glutathione S-Transferase: Evidence for Incorporation of an On-Face (π···HO−Ar) Hydrogen Bond at Tyrosine-9
  Biochemistry, 1996
• Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate
  Structure, 1995
• Structure Determination and Refinement of Human Alpha Class Glutathione Transferase A1-1, and a Comparison with the Mu and Pi Class Enzymes
  Journal of Molecular Biology, 1993
• Mutation of an evolutionarily conserved tyrosine residue in the active site of a human class Alpha glutathione transferase
  FEBS Letters, 1991
• Determination of the microscopic rate constants for the base catalyzed conjugation of 5-androstene-3,17-dione
  Journal of the American Chemical Society, 1989
• Amino acid substitutions in the human glutathione S-transferases confer different specificities in the prostaglandin endoperoxide conversion pathway
  Biochemical and Biophysical Research Communications, 1989