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
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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 $\rightleftharpoons$ 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.