Alpha,alpha-trehalose synthase
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Alpha,alpha-trehalose synthase
Alpha,alpha-trehalose synthase

Alpha,alpha-trehalose synthase | |||||||||
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Identifiers | |||||||||
EC number | 2.4.1.245 [4] | ||||||||
Databases | |||||||||
IntEnz | IntEnz view [5] | ||||||||
BRENDA | BRENDA entry [6] | ||||||||
ExPASy | NiceZyme view [7] | ||||||||
KEGG | KEGG entry [8] | ||||||||
MetaCyc | metabolic pathway [9] | ||||||||
PRIAM | profile [10] | ||||||||
PDB structures | RCSB PDB [11] PDBe [12] PDBsum [13] | ||||||||
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Search | |||||||||
PMC | articles [14] | ||||||||
PubMed | articles [15] | ||||||||
NCBI | proteins [16] |
Alpha,alpha-trehalose synthase (EC 2.4.1.245 [17] , 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
This enzyme requires Mg2+ for maximal activity.
Alpha,alpha-trehalose synthase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 2.4.1.245 [4] | ||||||||
Databases | |||||||||
IntEnz | IntEnz view [5] | ||||||||
BRENDA | BRENDA entry [6] | ||||||||
ExPASy | NiceZyme view [7] | ||||||||
KEGG | KEGG entry [8] | ||||||||
MetaCyc | metabolic pathway [9] | ||||||||
PRIAM | profile [10] | ||||||||
PDB structures | RCSB PDB [11] PDBe [12] PDBsum [13] | ||||||||
| |||||||||
Search | |||||||||
PMC | articles [14] | ||||||||
PubMed | articles [15] | ||||||||
NCBI | proteins [16] |
References
[1]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/15364950Qu 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.
Sep 19, 2019, 7:25 PM
[2]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/15737605Ryu 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.
Sep 19, 2019, 7:25 PM