Alpha,alpha-trehalose phosphorylase (configuration-retaining)
(Redirected from A,a-trehalose phosphorylase (configuration-retaining))
| Alpha,alpha-trehalose phosphorylase (configuration-retaining) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.231 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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].
References
[edit]- 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 (Pt 2): 335–40. doi:10.1042/0264-6021:3630335. PMC 1222483. 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 (Pt 3): 757–67. doi:10.1042/0264-6021:3560757. PMC 1221902. 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 (Pt 3): 727–36. doi:10.1042/0264-6021:3600727. PMC 1222278. PMID 11736665.
