Alpha,alpha-trehalose phosphorylase (configuration-retaining)

Alpha,alpha-trehalose phosphorylase (configuration-retaining)
Identifiers
EC number 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

    • 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.


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