Alpha,alpha-trehalose synthase
| Alpha,alpha-trehalose synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.245 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alpha,alpha-trehalose synthase (EC 2.4.1.245, trehalose synthase, trehalose synthetase, UDP-glucose:glucose 1-glucosyltransferase, TreT, PhGT) is an enzyme with systematic name ADP-glucose:D-glucose 1-alpha-D-glucosyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- ADP-glucose + D-glucose alpha,alpha-trehalose + ADP
This enzyme requires Mg2+ for maximal activity.
References
- ^ Qu Q, Lee SJ, Boos W (November 2004). "TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis". The Journal of Biological Chemistry. 279 (46): 47890–7. doi:10.1074/jbc.m404955200. PMID 15364950.
- ^ Ryu SI, Park CS, Cha J, Woo EJ, Lee SB (April 2005). "A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization". Biochemical and Biophysical Research Communications. 329 (2): 429–36. doi:10.1016/j.bbrc.2005.01.149. PMID 15737605.
External links
- Alpha,alpha-trehalose+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
