Enzyme

Download
EC Tree
     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.231
Description:Alpha,alpha-trehalose phosphorylase (configuration-retaining).
Alternative Name: Trehalose phosphorylase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.231
BRENDA Enzyme Link: BRENDA 2.4.1.231
KEGG Enzyme Link: KEGG2.4.1.231
BioCyc Enzyme Link: BioCyc 2.4.1.231
ExPASy Enzyme Link: ExPASy2.4.1.231
EC2PDB Enzyme Link: EC2PDB 2.4.1.231
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.231
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.231
IntEnz Enzyme Link: IntEnz 2.4.1.231
MEDLINE Enzyme Link: MEDLINE 2.4.1.231
MSA:

2.4.1.231;

Phylogenetic Tree:

2.4.1.231;

Uniprot:
M-CSA:
RHEA:16257 alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and characterization of trehalose phosphorylase from the commercial mushroom Agaricus bisporus.Wannet WJ, Op den Camp HJ, Wisselink HW, van der Drift C, Van Griensven LJ, Vogels GD1998 Sep 169813313
Purification and characterization of a trehalose synthase from the basidiomycete grifola frondosa Saito K, Kase T, Takahashi E, Horinouchi S1998 Nov9797287
Production of trehalose synthase from a basidiomycete, Grifola frondosa, in Escherichia coli.Saito K, Yamazaki H, Ohnishi Y, Fujimoto S, Takahashi E, Horinouchi S1998 Aug9763690
Studying non-covalent enzyme carbohydrate interactions by STD NMR.Brecker L, Schwarz A, Goedl C, Kratzer R, Tyl CE, Nidetzky B2008 Aug 1118281024
Cloning and characterization of a gene encoding trehalose phosphorylase (TP) from Pleurotus sajor-caju.Han SE, Kwon HB, Lee SB, Yi BY, Murayama I, Kitamoto Y, Byun MO2003 Aug12880768
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.Eis C, Nidetzky B2002 Apr 1511931662
Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.Nidetzky B, Eis C2001 Dec 1511736665
Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.Eis C, Watkins M, Prohaska T, Nidetzky B2001 Jun 1511389683
Characterization of trehalose phosphorylase from Schizophyllum commune.Eis C, Nidetzky B1999 Jul 1510393097