| EC |
2.4.1.231 |
| Accepted name: |
α,α-trehalose phosphorylase (configuration-retaining) |
| Reaction: |
α,α-trehalose + phosphate = α-D-glucose + α-D-glucose 1-phosphate |
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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 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 |
| 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] |
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| [EC 2.4.1.231 created 2003] |
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