Alpha,alpha-trehalose phosphorylase (configuration-retaining)
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In enzymology, an alpha,alpha-trehalose phosphorylase (configuration-retaining) (EC 2.4.1.231) is an enzyme that catalyzes the chemical reaction
- alpha,alpha-trehalose + phosphate alpha-D-glucose + alpha-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are alpha,alpha-trehalose and phosphate, whereas its two products are alpha-D-glucose and alpha-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is alpha,alpha-trehalose:phosphate alpha-D-glucosyltransferase. This enzyme is also called trehalose phosphorylase[ambiguous].
[edit] References
- IUBMB entry for 2.4.1.231
- BRENDA references for 2.4.1.231 (Recommended.)
- PubMed references for 2.4.1.231
- PubMed Central references for 2.4.1.231
- Google Scholar references for 2.4.1.231
- Eis C, Nidetzky B (2002). "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: 335–40. doi: . PMID 11931662.
- Eis C, Watkins M, Prohaska T, Nidetzky B (2001). "Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune". Biochem. J. 356: 757–67. doi: . PMID 11389683.
- Nidetzky B, Eis C (2001). "Alpha-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: 727–36. doi: . PMID 11736665.