IUBMB Enzyme Nomenclature


Accepted name: α,α-trehalose phosphorylase (configuration-retaining)

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, 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:


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]

Return to EC 2.4.1 home page
Return to EC 2.4 home page
Return to EC 2 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page