α,α-trehalose synthase from Creative Enzymes

Requires Mg2+ for maximal activity. The enzyme-catalysed reaction is reversible. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-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-α-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose