A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis

Gelijkaardige items

• The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase
  door: Vararattanavech, Ardcharaporn, et al.
  Gepubliceerd in: (2005)
• Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases
  door: Winayanuwattikun, Pakorn, et al.
  Gepubliceerd in: (2007)
• Catalytic and structural contributions for glutathione-binding residues in a Delta class glutathione S-transferase
  door: Winayanuwattikun, Pakorn, et al.
  Gepubliceerd in: (2004)
• Glutathione transferase mimics: micellar catalysis of an enzymic reaction.
  door: Lindkvist, B, et al.
  Gepubliceerd in: (1997)
• Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
  door: Wongsantichon, Jantana, et al.
  Gepubliceerd in: (2015)