KEGG   ENZYME: 2.4.1.231Help
Entry
EC 2.4.1.231                Enzyme                                 

Name
alpha,alpha-trehalose phosphorylase (configuration-retaining);
trehalose phosphorylase[ambiguous]
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
alpha,alpha-trehalose:phosphate alpha-D-glucosyltransferase
Reaction(IUBMB)
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate [RN:R07265]
Reaction(KEGG)
Substrate
alpha,alpha-trehalose [CPD:C01083];
phosphate [CPD:C00009]
Product
alpha-D-glucose [CPD:C00267];
alpha-D-glucose 1-phosphate [CPD:C00103]
Comment
Unlike EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
History
EC 2.4.1.231 created 2003
Reference
1  [PMID:11931662]
  Authors
Eis C, Nidetzky B.
  Title
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.
  Journal
Biochem. J. 363 (2002) 335-40.
  Organism
Schizophyllum commune
Reference
2  [PMID:11389683]
  Authors
Eis C, Watkins M, Prohaska T, Nidetzky B.
  Title
Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.
  Journal
Biochem. J. 356 (2001) 757-67.
  Organism
Schizophyllum commune
Reference
3  [PMID:11736665]
  Authors
Nidetzky B, Eis C.
  Title
Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.
  Journal
Biochem. J. 360 (2001) 727-36.
  Organism
Schizophyllum commune
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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