2.4.1.245: alpha,alpha-trehalose synthase
This is an abbreviated version!
For detailed information about alpha,alpha-trehalose synthase, go to the full flat file.
Reaction
Synonyms
PH1035, TaTS, TmTreT, trehalose glycosyltransferring synthase, Trehalose synthase, TreT
ECTree
2.4.1.245 alpha,alpha-trehalose synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.4.1.245 - alpha,alpha-trehalose synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-trehalose
-
-
-
r
alpha,alpha-trehalose + CDP
CDP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
r
UDP-alpha-D-glucose + D-fructose
?
-
the enzyme employs a glucose acceptor with the highest preference and other monosaccharides (D-fructose, D-mannose) with less affinities acceptors. The trehalose analogue containing mannose is produced with approximately 70% of trehalose production and a two-fold greater amount than the analogue containing a fructose for the 12-24 h reaction
-
-
r
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
-
-
-
?
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
100% activity
-
-
?
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
-
-
-
-
r
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
-
10% activity with ADP-glucose compared to UDP-glucose
-
-
r
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
Thermoproteus tenax Kra 1 / DSM 2078
-
10% activity with ADP-glucose compared to UDP-glucose
-
-
r
ADP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + ADP
-
GDP-alpha-D-glucose is the most favored in terms of reaction specificity, kcat/Km. UDP-alpha-D-glucose and ADP-alpha-D-glucose are employed with less preferences. The enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
ADP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + ADP
-
-
-
-
r
alpha,alpha-trehalose + ADP
ADP-alpha-D-glucose + D-glucose
-
the enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
alpha,alpha-trehalose + ADP
ADP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
r
alpha,alpha-trehalose + ADP
ADP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
r
alpha,alpha-trehalose + GDP
GDP-alpha-D-glucose + D-glucose
-
the enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
alpha,alpha-trehalose + GDP
GDP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
?
alpha,alpha-trehalose + GDP
GDP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
?
alpha,alpha-trehalose + UDP
UDP-alpha-D-glucose + D-glucose
-
the enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
alpha,alpha-trehalose + UDP
UDP-alpha-D-glucose + D-glucose
-
both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
?
GDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + GDP
-
GDP-alpha-D-glucose is the most favored in terms of reaction specificity, kcat/Km. UDP-alpha-D-glucose and ADP-alpha-D-glucose are employed with less preferences. The enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
GDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + GDP
48.2% activity compared to ADP-glucose
-
-
?
GDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + GDP
-
5% of the efficiency with ADP-glucose
-
-
r
UDP-alpha-D-glucose + D-galactose
alpha-D-Glc-(1->1)-alpha-D-Glc + UDP
-
-
-
?
UDP-alpha-D-glucose + D-galactose
alpha-D-Glc-(1->1)-alpha-D-Glc + UDP
-
-
-
?
UDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + UDP
-
-
-
?
UDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + UDP
-
GDP-alpha-D-glucose is the most favored in terms of reaction specificity, kcat/Km. UDP-alpha-D-glucose and ADP-alpha-D-glucose are employed with less preferences. The enzyme reversely cleaves alpha,alpha-trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-alpha-D-glucose. Although ADP-alpha-D-glucose is the least favorable donor, the counterpart, ADP, is the most favorable acceptor for the reverse synthesis of NDP-alpha-D-glucose in kcat/Km. GDP and UDP are less preferred, compared to ADP
-
-
r
UDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + UDP
-
-
-
?
UDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + UDP
-
the purified soluble enzyme, as well as the glutathione-S-transferase-fusion enzyme, show the catalytic specificity for synthesizing trehalose from UDP-alpha-D-glucose as the donor and glucose as the acceptor. The enzyme employs a glucose acceptor with the highest preference and other monosaccharides (D-fructose, D-mannose) with less affinities acceptors. Both soluble and glutathione-S-transferase-fusion enzymes have the greatest preference for ADP as the acceptor substrate in the synthesis of NDP-Glc, and they also employ GDP, UDP, and CDP as less favorable substrates, approximately in this order
-
-
r
UDP-alpha-D-glucose + D-mannose
?
-
the enzyme employs a glucose acceptor with the highest preference and other monosaccharides (D-fructose, D-mannose) with less affinities acceptors. The trehalose analogue containing mannose is produced with approximately 70% of trehalose production and a two-fold greater amount than the analogue containing a fructose for the 12-24 h reaction
-
-
r
UDP-alpha-D-glucose + D-mannose
?
-
the enzyme employs a glucose acceptor with the highest preference and other monosaccharides (D-fructose, D-mannose) with less affinities acceptors. The trehalose analogue containing mannose is produced with approximately 70% of trehalose production and a two-fold greater amount than the analogue containing a fructose for the 12-24 h reaction
-
-
r
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
32.7% activity compared to ADP-glucose
-
-
?
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
-
6% of the efficiency with ADP-glucose
-
-
r
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
-
clear preference for UDP-glucose over ADP-glucose
-
-
r
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
Thermoproteus tenax Kra 1 / DSM 2078
-
clear preference for UDP-glucose over ADP-glucose
-
-
r
additional information
?
-
UDP-glucose is as efficient as ADP-glucose and GDP-glucose
-
-
?
additional information
?
-
molecular basis of the synthetic mechanism of trehalose, or the nucleotide sugar in the reverse reaction of TreT. TreT can utilize ADP-glucose and GDP-glucose as well as UDP-glucose to synthesize trehalose, the nucleotide sugar molecule is recognized by the nucleotide-sensing Gly-Gly-Leu motif that is located at the domain interface in many GT-B family members, and TreT contains this motif at residues 52-55, the acceptor molecule binds predominantly to the N-terminal domain
-
-
?
additional information
?
-
-
molecular basis of the synthetic mechanism of trehalose, or the nucleotide sugar in the reverse reaction of TreT. TreT can utilize ADP-glucose and GDP-glucose as well as UDP-glucose to synthesize trehalose, the nucleotide sugar molecule is recognized by the nucleotide-sensing Gly-Gly-Leu motif that is located at the domain interface in many GT-B family members, and TreT contains this motif at residues 52-55, the acceptor molecule binds predominantly to the N-terminal domain
-
-
?
additional information
?
-
-
reaction is reversible, formation of trehalose is favored by rate of reaction and equilibrium. No substrate: glucose 1-phosphate, glucose 6-phosphate, fructose, mannose, galactose, xylose, 2-deoxyglucose, glucosamine, alpha-methylglucoside, sorbitol
-
-
?
additional information
?
-
-
no activity with maltose and glucose 1-phosphate
-
-
?
additional information
?
-
Thermoproteus tenax Kra 1 / DSM 2078
-
no activity with maltose and glucose 1-phosphate
-
-
?
additional information
?
-
-
the enzyme does not utilize galactose as an acceptor
-
-
?
additional information
?
-
-
the enzyme does not utilize galactose as an acceptor
-
-
?
