The Enzyme Database

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Accepted name: α,α-trehalose phosphorylase (configuration-retaining)
Reaction: α,α-trehalose + phosphate = α-D-glucose + α-D-glucose 1-phosphate
For diagram of the reactions of trehalose phosphorylase, click here
Other name(s): trehalose phosphorylase[ambiguous]
Systematic name: α,α-trehalose:phosphate α-D-glucosyltransferase
Comments: Unlike EC, 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
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]
[EC created 2003]

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