×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

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 2X6Q
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.
CATH-Gene3D is a Global Biodata Core Resource Learn more...