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ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-1,1-trehalose
ADP-alpha-D-glucose + D-glucose
ADP + alpha,alpha-trehalose
-
-
-
r
ADP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + ADP
alpha,alpha-1,1-trehalose + ADP
ADP-glucose + D-glucose
-
-
-
-
r
alpha,alpha-trehalose + ADP
ADP-alpha-D-glucose + D-glucose
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
alpha,alpha-trehalose + GDP
GDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + UDP
UDP-alpha-D-glucose + D-glucose
CDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + CDP
-
-
-
-
r
GDP-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + GDP
GDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + GDP
GDP-glucose + D-glucose
alpha,alpha-trehalose + GDP
-
-
-
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
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-mannose
?
UDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + UDP
UDP-glucose + D-glucose
alpha,alpha-trehalose + UDP
-
-
-
r
additional information
?
-
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
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-alpha-D-glucose + D-glucose
alpha,alpha-trehalose + GDP
-
-
-
-
r
GDP-glucose + D-glucose
alpha,alpha-1,1-trehalose + GDP
-
-
-
?
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
-
-
-
?
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
-
-
?
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Ryu, S.I.; Park, C.S.; Cha, J.; Woo, E.J.; Lee, S.B.
A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: Molecular cloning and characterization
Biochem. Biophys. Res. Commun.
329
429-436
2005
Pyrococcus horikoshii (O58762)
brenda
Qu, Q.; Lee, S-J.; Boos, W.
TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis
J. Biol. Chem.
279
47890-47897
2004
Thermococcus litoralis
brenda
Kouril, T.; Zaparty, M.; Marrero, J.; Brinkmann, H.; Siebers, B.
A novel trehalose synthesizing pathway in the hyperthermophilic crenarchaeon Thermoproteus tenax: the unidirectional TreT pathway
Arch. Microbiol.
190
355-369
2008
Thermoproteus tenax, Thermoproteus tenax Kra 1 / DSM 2078
brenda
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)
brenda
Ryu, S.I.; Woo, J.B.; Lee, S.B.
Coupling reactions of trehalose synthase from Pyrococcus horikoshii: Cost-effective synthesis and anti-adhesive activity of beta-galactosyl oligosaccharides using a one-pot three-enzyme system with trehalose
Biores. Technol.
136
743-746
2013
Pyrococcus horikoshii (O58762)
brenda
Woo, E.J.; Ryu, S.I.; Song, H.N.; Jung, T.Y.; Yeon, S.M.; Lee, H.A.; Park, B.C.; Park, K.H.; Lee, S.B.
Structural insights on the new mechanism of trehalose synthesis by trehalose synthase TreT from Pyrococcus horikoshii
J. Mol. Biol.
404
247-259
2010
Pyrococcus horikoshii (O58762), Pyrococcus horikoshii
brenda
Ryu, S.; Kim, J.; Kim, E.; Chung, S.; Lee, S.
Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: Efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling
Process Biochem.
46
128-134
2011
Pyrococcus horikoshii
-
brenda
Qu, M.; Du, J.; Chen, W.
Optimization of the medium composition using response surface methodology for production of trehalose synthase from Corynebacterium glutamicum
J. Pure Appl. Microbiol.
8
231-238
2014
Corynebacterium glutamicum
-
brenda
Kim, H.; Chang, Y.; Ryu, S.; Moon, S.; Lee, S.
Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase Inhibitory effects on several disaccharidase activities
J. Mol. Catal. B
49
98-103
2007
Pyrococcus horikoshii (O58762), Pyrococcus horikoshii OT-3 (O58762)
-
brenda
Ryu, S.; Kim, J.; Huong, N.; Woo, E.; Moon, S.; Lee, S.
Molecular cloning and characterization of trehalose synthase from Thermotoga maritima DSM3109 Syntheses of trehalose disaccharide analogues and NDP-glucoses
Enzyme Microb. Technol.
47
249-256
2010
Thermotoga maritima, Thermotoga maritima DSM 3109
-
brenda
Lin, Y.F.; Su, P.C.; Chen, P.T.
Production and characterization of a recombinant thermophilic trehalose synthase from Thermus antranikianii
J. Biosci. Bioeng.
129
418-422
2020
Thermus antranikianii (WP_028494267)
brenda