Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.

Lignende værker

• Characterization of trehalose phosphorylase from Schizophyllum commune.
  af: Eis, C, et al.
  Udgivet: (1999)
• Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors.
  af: Eis, Christian, et al.
  Udgivet: (2002)
• Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.
  af: Eis, C, et al.
  Udgivet: (2001)
• Structure–function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
  af: Goedl, Christiane, et al.
  Udgivet: (2006)
• Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda.
  af: Nidetzky, B, et al.
  Udgivet: (2000)