Alpha,alpha-trehalose phosphorylase (configuration-retaining)
| Alpha,alpha-trehalose phosphorylase (configuration-retaining) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.231 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Alpha,alpha-trehalose phosphorylase (configuration-retaining) (EC 2.4.1.231) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme characterised from the fungus Schizophyllum commune are trehalose and orthophosphate (Pi). Its products are α-D-glucose and α-D-glucose 1-phosphate. The reaction is reversible and preserves the stereochemistry at the anomeric centre.[1][2][3]
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. It is also called trehalose phosphorylase[ambiguous].[4]
References
- ↑ 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.
- ↑ 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.
- ↑ Enzyme 2.4.1.231 at KEGG Pathway Database.
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