CATH Classification

Domain Context

CATH Clusters

Superfamily Glycogen Phosphorylase B;
Functional Family

Enzyme Information

2.4.1.245
Alpha,alpha-trehalose synthase.
based on mapping to UniProt O58762
NDP-alpha-D-glucose + D-glucose = alpha,alpha-trehalose + NDP.
-!- The enzyme-catalyzed reaction is reversible. -!- In the reverse direction to that shown above, the enzyme is specific for alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose. -!- While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-alpha-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-alpha-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-alpha-D-glucose. -!- Formerly EC 2.4.1.n1.

UniProtKB Entries (1)

O58762
TRET_PYRHO
Pyrococcus horikoshii OT3
Trehalose synthase

PDB Structure

PDB 2X6R
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Insights on the New Mechanism of Trehalose Synthesis by Trehalose Synthase Tret from Pyrococcus Horikoshii.
Woo, E.-J., Ryu, S., Song, H.-N., Jung, T.-Y., Yeon, S., Lee, H., Park, B.C., Park, K., Lee, S.-B.
J.Mol.Biol.