KEGG   ENZYME: 2.4.1.245Help
Entry
EC 2.4.1.245                Enzyme                                 

Name
alpha,alpha-trehalose synthase;
trehalose synthase;
trehalose synthetase;
UDP-glucose:glucose 1-glucosyltransferase;
TreT;
PhGT;
ADP-glucose:D-glucose 1-alpha-D-glucosyltransferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
NDP-alpha-D-glucose:D-glucose 1-alpha-D-glucosyltransferase
Reaction(IUBMB)
NDP-alpha-D-glucose + D-glucose = alpha,alpha-trehalose + NDP [RN:R10525]
Reaction(KEGG)
Substrate
NDP-alpha-D-glucose [CPD:C15541];
D-glucose [CPD:C00031]
Product
alpha,alpha-trehalose [CPD:C01083];
NDP [CPD:C00454]
Comment
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 alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-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-alpha-D-glucose to the same extent [2,3], that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-alpha-D-glucose [1] and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-alpha-D-glucose [4].
History
EC 2.4.1.245 created 2008, modified 2013
Pathway
Starch and sucrose metabolism
Metabolic pathways
Orthology
K13057  
trehalose synthase
Genes
NHL: 
TEE: 
GEO: 
Geob_2843(treT)
GEB: 
PCA: 
Pcar_3111(treT)
DRT: 
DAK: 
DPR: 
AFW: 
MXA: 
MFU: 
MSD: 
MYM: 
CCX: 
AGE: 
VIN: 
SAMY: 
LLU: 
HOH: 
SAT: 
DAO: 
DTI: 
SFU: 
DAV: 
NGL: 
MCG: 
NPP: 
AFE: 
AFR: 
DKU: 
DGI: 
TJR: 
TPZ: 
CPO: 
LPIL: 
SALS: 
SCX: 
AMS: 
ACTN: 
ACQ: 
AOS: 
ARD: 
RXY: 
CWO: 
TRO: 
STI: 
TTR: 
PUV: 
EMI: 
TAI: 
ACO: 
AMO: 
RBI: 
MRS: 
HTH: 
HTE: 
TTK: 
TST_0833(treT)
TMA: 
TMM: 
TMI: 
TMW: 
TMQ: 
TMX: 
TPT: 
TRQ: 
TNA: 
TNP: 
THQ: 
THZ: 
THR: 
TLE: 
TTA: 
PHY: 
TME: 
TAF: 
FNO: 
FPE: 
FIA: 
KOL: 
KPF: 
MPG: 
CEX: 
NDE: 
NMV: 
TID: 
TOP: 
TCM: 
MTP: 
MEM: 
MBG: 
MEMA: 
MMAB1_0304(treT) MMAB1_0814(treT) MMAB1_1593(treT)
NMG: 
HXA: 
NGE: 
HRU: 
NOU: 
PHO: 
PH1035(PH1035)
PFU: 
PFI: 
PYS: 
TSI: 
TBA: 
TLT: 
THS: 
TEU: 
TGY: 
PPAC: 
SMR: 
SHC: 
SSO: 
SOL: 
SSOA: 
SSOL: 
SSOF: 
STO: 
SAI: 
SACN: 
SACR: 
SACS: 
SIS: 
SIA: 
SIM: 
SID: 
SIY: 
SIN: 
SII: 
SIH: 
SIR: 
SIC: 
MSE: 
MCN: 
AHO: 
PAI: 
PCL: 
PAS: 
PYR: 
POG: 
PYW: 
TUZ: 
TTN: 
TTX_0217(treT)
TPE: 
THF: 
 » show all
Taxonomy
Reference
1  [PMID:15364950]
  Authors
Qu Q, Lee SJ, Boos W.
  Title
TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis.
  Journal
J. Biol. Chem. 279 (2004) 47890-7.
  Sequence
[tlt:OCC_03547]
Reference
2  [PMID:15737605]
  Authors
Ryu SI, Park CS, Cha J, Woo EJ, Lee SB.
  Title
A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization.
  Journal
Biochem. Biophys. Res. Commun. 329 (2005) 429-36.
  Sequence
[pho:PH1035]
Reference
3  [PMID:18835983]
  Authors
Nobre A, Alarico S, Fernandes C, Empadinhas N, da Costa MS
  Title
A unique combination of genetic systems for the synthesis of trehalose in Rubrobacter xylanophilus: properties of a rare actinobacterial TreT.
  Journal
J. Bacteriol. 190 (2008) 7939-46.
  Sequence
[rxy:Rxyl_2973]
Reference
4  [PMID:18483808]
  Authors
Kouril T, Zaparty M, Marrero J, Brinkmann H, Siebers B
  Title
A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway.
  Journal
Arch. Microbiol. 190 (2008) 355-69.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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