Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases

Antzeko izenburuak

• Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase
  nork: Winayanuwattikun, Pakorn, et al.
  Argitaratua: (2004)
• A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis
  nork: Vararattanavech, Ardcharaporn, et al.
  Argitaratua: (2007)
• Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1.
  nork: Allocati, Nerino, et al.
  Argitaratua: (2002)
• Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions
  nork: Piromjitpong, Juthamart, et al.
  Argitaratua: (2007)
• Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
  nork: Wongsantichon, Jantana, et al.
  Argitaratua: (2015)