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Information on EC 2.4.1.245 - alpha,alpha-trehalose synthase and Organism(s) Rubrobacter xylanophilus and UniProt Accession Q1ARU5

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.245 alpha,alpha-trehalose synthase
IUBMB Comments
Requires Mg2+ for maximal activity . The enzyme-catalysed reaction is reversible . 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 . 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 and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-alpha-D-glucose .
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Rubrobacter xylanophilus
UNIPROT: Q1ARU5
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The taxonomic range for the selected organisms is: Rubrobacter xylanophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trehalose glycosyltransferring synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trehalose glycosyltransferring synthase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
NDP-alpha-D-glucose:D-glucose 1-alpha-D-glucosyltransferase
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].
CAS REGISTRY NUMBER
COMMENTARY hide
126341-88-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
show the reaction diagram
100% activity
-
-
?
GDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + GDP
show the reaction diagram
48.2% activity compared to ADP-glucose
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-
?
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
show the reaction diagram
32.7% activity compared to ADP-glucose
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
2 mM or 20 mM Ca2+ induces slightly enhanced activity
Fe3+
2 mM Fe3+ induces slightly enhanced activity
Li+
2 mM or 20 mM Li+ induces slightly enhanced activity
Mg2+
Mg2+ is required for activity, 20 mM Mg+ induces slightly enhanced activity
Mn2+
2 mM Mn2+ induces slightly enhanced activity
additional information
no enhanced activity in the presence of 20 mM Fe3+ or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8
ADP
recombinant enzyme, at 60°C
0.8
ADP-glucose
recombinant enzyme, at 60°C
82
alpha,alpha-1,1-trehalose
recombinant enzyme, at 60°C
1.3
D-glucose
recombinant enzyme, at 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PRD-1T (DSM 9941)
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46700
calculated from amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
the half-lives for inactivation at 60°C and at 70°C are 309 h and 4.1 h, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, Q-Sepharose fast-flow column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nobre, A.; Alarico, S.; Fernandes, C.; Empadinhas, N.; 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
7939-7946
2008
Rubrobacter xylanophilus (Q1ARU5)
Manually annotated by BRENDA team