Reaction: α,α-trehalose + phosphate = α-D-glucose + α-D-glucose 1-phosphate
For diagram of reaction click here
Other name(s): trehalose phosphorylase[ambiguous]
Systematic name: α,α-trehalose:phosphate α-D-glucosyltransferase
Comments: Unlike EC 2.4.1.64, α,α-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Eis, C. and Nidetzky, B. 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. Biochem. J. 363 (2002) 335-340. [PMID: 11931662]
2. Eis, C., Watkins, M., Prohaska, T. and Nidetzky, B. Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem. J. 356 (2001) 757-767. [PMID: 11389683]
3. Nidetzky, B. and Eis, C. α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem. J. 360 (2001) 727-736. [PMID: 11736665]