Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.

Eitemau Tebyg

• Characterization of trehalose phosphorylase from Schizophyllum commune.
  gan: Eis, C, et al.
  Cyhoeddwyd: (1999)
• Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.
  gan: Nidetzky, B, et al.
  Cyhoeddwyd: (2001)
• 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.
  gan: Eis, Christian, et al.
  Cyhoeddwyd: (2002)
• Structure–function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
  gan: Goedl, Christiane, et al.
  Cyhoeddwyd: (2006)
• Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda.
  gan: Nidetzky, B, et al.
  Cyhoeddwyd: (2000)