The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.4.1.245     
Accepted name: α,α-trehalose synthase
Reaction: NDP-α-D-glucose + D-glucose = α,α-trehalose + NDP
Glossary: NDP = a nucleoside diphosphate
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT; ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Systematic name: NDP-α-D-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. 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 [1]. 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 [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-α-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-α-D-glucose [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [DOI] [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [DOI] [PMID: 15737605]
3.  Nobre, A., Alarico, S., Fernandes, C., Empadinhas, N. and da Costa, M.S. A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT. J. Bacteriol. 190 (2008) 7939–7946. [DOI] [PMID: 18835983]
4.  Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H. and Siebers, B. A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway. Arch. Microbiol. 190 (2008) 355–369. [DOI] [PMID: 18483808]
[EC 2.4.1.245 created 2008, modified 2013]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald