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maltose = alpha,alpha-trehalose
maltose = alpha,alpha-trehalose
-
-
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement catalytic mechanism, overview
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
-
-
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alpha,alpha-trehalose
maltose
high-maltose rice syrup
alpha,alpha-trehalose
-
-
the highest alpha,alpha-trehalose yield (54.6%) can be obtained by 3.5 units/maltose (g) of trehalose synthase from the maltose syrup at 50°C for 20-24 h
-
?
maltose
alpha,alpha-trehalose
maltose
alpha,alpha-trehalose + D-glucose + maltose
starch
alpha,alpha-trehalose
-
substrate of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
-
-
?
sucrose
D-glucose + D-fructose + [alpha-D-glucopyranosyl-(1,1)-D-fructofuranose]
-
low activity on sucrose
-
-
?
sucrose
trehalulose
-
activity is very low compared to that with maltose
i.e. 1-O-alpha-D-glucopyranosyl-D-fructose
?
additional information
?
-
alpha,alpha-trehalose
maltose
-
-
-
?
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
?
alpha,alpha-trehalose
maltose
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
?
alpha,alpha-trehalose
maltose
composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
WP_028494267
1.48fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
?
alpha,alpha-trehalose
maltose
-
-
-
r
alpha,alpha-trehalose
maltose
-
-
-
?
maltose
alpha,alpha-trehalose
conversion of trehalose from maltose is 43.62%. At the same time, TreS produces about 23.85% glucose as a by product after 10 h of incubation
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
the maximum conversion yield reaches 69% at 25°C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
-
the maximum conversion yield reaches 69% at 25°C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
wild-type, 92% yield
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
an enzymatic intramolecular rearrangement reaction
-
-
r
maltose
alpha,alpha-trehalose
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
an enzymatic intramolecular rearrangement reaction
-
-
r
maltose
alpha,alpha-trehalose
bioconversions results in final trehalose levels of 60%. The enzyme produces reduced amounts of the byproduct glucose (15%)
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose. Maximum conversion rate for maltose into trehalose is independent of substrate concentration and reaches 71% at 20°C
-
-
r
maltose
alpha,alpha-trehalose
-
one-step conversion via intramolecular transglucosylation reaction
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
r
-
?
maltose
alpha,alpha-trehalose
-
r
-
?
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
30% yield
-
?
maltose
alpha,alpha-trehalose
conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
bioconversions results in final trehalose levels of 60%. The enzyme produces reduced amounts of the byproduct glucose (10%)
-
-
?
maltose
alpha,alpha-trehalose
composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
WP_028494267
1.48fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
?
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
wild-type, 80% yield
-
?
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
r
maltose
alpha,alpha-trehalose
-
-
-
-
r
maltose
alpha,alpha-trehalose
-
the recombinant enzyme has a 4.1fold higher catalytic efficientcy for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose + D-glucose + maltose
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
maltose
alpha,alpha-trehalose + D-glucose + maltose
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
additional information
?
-
does not use acarbose and glucose as substrates
-
-
?
additional information
?
-
does not use acarbose and glucose as substrates
-
-
?
additional information
?
-
the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 59-69% trehalose from 15 mM maltose at 25-35°C in 4-9 h with 14.4-21.7% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 56.8-60.4% trehalose from 300 mM maltose at 40°C in 16-24 h with 7.3-8.6% D-glucose by-product
-
-
?
additional information
?
-
modeling of maltose into the active site, overview
-
-
?
additional information
?
-
-
modeling of maltose into the active site, overview
-
-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
-
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change
-
-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 58.2% trehalose from 300 mM maltose at 30°C in 24 h with 7.1% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 92% trehalose from 800 mM maltose at 5°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 48% trehalose from 100 mM maltose at 37°C
-
-
?
additional information
?
-
the enzyme yields 48% trehalose from 100 mM maltose at 37°C
-
-
?
additional information
?
-
the enzyme yields 61-64% trehalose from 60 mM maltose at 20-30°C in 24 h with 2.3-4.5% D-glucose by-product
-
-
?
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
?
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of alpha-aryl glucosides as well as alpha-glucosyl fluoride, overview. Reaction of TreS with 5-fluoro-alpha-D-glucosyl fluoride results in the trapping of a covalent glycosyl-enzyme intermediate consistent with TreS being a member of the retaining glycoside hydrolase family 13 enzyme family, thus likely following a two-step, double displacement mechanism. Inability of TreS to incorporate isotope-labeled exogenous glucose into maltose or trehalose, the absence of a secondary deuterium kinetic isotope effect and the general independence of kcat upon leaving group ability both point to a rate-determining conformational change, likely the opening and closing of the enzyme active site
-
-
?
additional information
?
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
?
additional information
?
-
the enzyme yields 59.5% trehalose from 90 mM maltose at 30°C in 8 h with 13.2% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product
-
-
?
additional information
?
-
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
-
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose
-
-
?
additional information
?
-
the enzyme yields 50-71% trehalose from 150 mM maltose at 20-60°C in 72 h with 3.6-19.2% D-glucose by-product
-
-
?
additional information
?
-
-
no substrates: glucose, fructose, lactose, sucrose, starch
-
-
?
additional information
?
-
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
?
additional information
?
-
optimal activity of purified recombinant enzyme at 30% substrate concentration
-
-
?
additional information
?
-
optimal activity of purified recombinant enzyme at 30% substrate concentration
-
-
?
additional information
?
-
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
?
additional information
?
-
the enzyme yields 70% trehalose from 100 mM maltose at 37°C in 12 h with 8.0% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 75% trehalose from 580 mM maltose at 15°C in 19 h without D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 67% trehalose from 90 mM maltose at 25°C with 12% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose from 150 mM maltose at 45°C in 10 h
-
-
?
additional information
?
-
the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 55-65% trehalose from 440 mM maltose at 25°C in 24 h with 10-15% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product
-
-
?
additional information
?
-
the enzyme yields 70% trehalose at 35°C with 8% D-glucose by-product
-
-
?
additional information
?
-
-
improvement of activity by reaction condition optimization for trehalose production, overview. Pressure as a stress condition can significantly increase the activity of intracellular enzyme TSase in Thermus aquaticus
-
-
?
additional information
?
-
-
improvement of activity by reaction condition optimization for trehalose production, overview. Pressure as a stress condition can significantly increase the activity of intracellular enzyme TSase in Thermus aquaticus
-
-
?
additional information
?
-
-
the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
-
-
?
additional information
?
-
the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
-
-
?
additional information
?
-
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
additional information
?
-
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
additional information
?
-
the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
-
-
?
additional information
?
-
the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
-
-
?
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5-fluoro-alpha-D-glucosyl fluoride
-
behaves like a reversible inhibitor
acarbose
competitively inhibited by the potent alpha-glucosidase inhibitor acarbose, acarbose-binding site structure, overview
beta-mercaptoethanol
complete inhibition at 1 mM
D-gluconohydroximino-1,5-lactam
-
-
D-glucose
in the presence of 10 mM D-glucose, TreS shows a 3.6fold increase in Km and a nearly unchanged Vmax for maltose, implying that D-glucose is a competitive inhibitor of TreS
dithiothreitol
9% inhibition at 5 mM, 12% at 10 mM
Fe3+
1 mM, 60% residual activity
Guanidine-HCl
-
complete inhibition at 1 M, 51% inhibition of aggregated enzyme
Na+
90% residual activity at 1 mM
sodium dodecylsulfate
-
1 mM, complete inhibition
sucrose
-
competitive inhibition of the interconversion between maltose and trehalose
Urea
-
90% inhibition at 2 M, 1% inhibition of aggregated enzyme
Al3+
98.5% inhibition at 1 mM
Al3+
complete inhibition at 2 mM
Al3+
-
complete inhibition at 2 mM, 8% inhibition of aggregated enzyme
Al3+
-
1 mM, complete inhibition
Ca2+
-
93% residual activity at 5 mM
Ca2+
13.4% inhibition at 10 mM, 9.5% at 1 mM
Ca2+
about 10% residual activity at 10 mM
Ca2+
-
the MTase activity of TreS is inhibited by 5 mM Ca2+ and other divalent cations
Ca2+
-
the MTase activity of TreS is inhibited by 5 mM Ca2+ and other divalent cations
Ca2+
98% residual activity at 5 mM
Ca2+
WP_028494267
10 mM, 29% loss of activity
Co2+
1 mM, 38% loss of activity
Co2+
1 mM, 55% residual activity
Co2+
17.2% inhibition at 1 mM
Co2+
about 5% residual activity at 10 mM
Co2+
WP_028494267
1 mM, 56% loss of activity
Cu2+
1 mM, complete inhibition
Cu2+
-
45.4% residual activity at 5 mM
Cu2+
1 mM, 5% residual activity
Cu2+
complete inhibition at 10 mM
Cu2+
52% residual activity at 1 mM
Cu2+
complete inhibition at 2 mM
Cu2+
-
complete inhibition at 2 mM, 23% inhibition of aggregated enzyme
Cu2+
complete inhibition at 5 mM
Cu2+
-
10 mM, 85% residual activity
Cu2+
34% inhibition at 1 mM, 41% at 10 mM
Cu2+
WP_028494267
1 mM, 83% loss of activity
Cu2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
EDTA
-
68.5% residual activity at 5 mM
EDTA
inhibitory above 1 mM
EDTA
15% inhibition at 1 mM, 35% at 10 mM
EDTA
86% residual activity at 5 mM
EDTA
46% inhibition at 1 mM, 100% at 10 mM
Fe2+
92% residual activity at 1 mM
Fe2+
complete inhibition at 2 mM
Fe2+
-
95% inhibition at 2 mM, 5% inhibition of aggregated enzyme
Hg2+
1 mM, 15% residual activity
Hg2+
complete inhibition at 1 mM
Hg2+
57% residual activity at 1 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Mg2+
1 mM, 75% residual activity
Mg2+
8.5% inhibition at 1-10 mM
Mg2+
92% residual activity at 5 mM
Mg2+
-
about 50% inhibition
Mn2+
-
60.9% residual activity at 5 mM
Mn2+
20% inhibition at 1 mM, 30% at 10 mM
Mn2+
about 10% residual activity at 10 mM
Mn2+
86% residual activity at 5 mM
Mn2+
-
10 mM, 60% residual activity
Ni2+
1 mM, 58% loss of activity
Ni2+
-
49.4% residual activity at 5 mM
Ni2+
28.5% inhibition at 1mM, 45% at 10 mM
Ni2+
about 10% residual activity at 10 mM
Ni2+
66% inhibition at 1 mM, 75% at 10 mM
Pb2+
-
-
Pb2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
SDS
-
0.25% residual activity at 5 mM
SDS
95.1% inhibition at 5 mM
SDS
10% residual activity at 1 mM
SDS
complete inhibition at 1 mM
SDS
77% inhibition at 1 mM, 100% at 10 mM
SDS
WP_028494267
1 mM, 99% loss of activity
Tris
10 mM, 9% residual activity
Tris
58% inhibition at 5 mM, 78% at 10 mM
Tris
the enzyme-Tris complex may represent a substrate-induced closed conformation that facilitates intramolecular isomerization and minimize disaccharide hydrolysis
Tris
-
complete inhibition at 25 mM, 23% inhibition of aggregated enzyme
Tris
structural characteristics of enzyme TtTS in complex with the inhibitor TriS
Tris
WP_028494267
1 mM, 46% loss of activity
Tris
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
validoxylamine
-
strong inhibition
validoxylamine
-
strong inhibition
Zn2+
1 mM, 67% loss of activity
Zn2+
-
71.6% residual activity at 5 mM
Zn2+
1 mM, 29% residual activity
Zn2+
complete inhibition at 5 mM
Zn2+
59% residual activity at 1 mM
Zn2+
complete inhibition at 2 mM
Zn2+
-
92% inhibition at 2 mM, 1% inhibition of aggregated enzyme
Zn2+
-
10 mM, 20% residual activity
Zn2+
WP_028494267
1 mM, 33% loss of activity
Zn2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
additional information
TreS activity is not affected by EDTA
-
additional information
-
TreS activity is not affected by EDTA
-
additional information
-
not inhibited by acarbose
-
additional information
-
not inhibited by acarbose
-
additional information
-
no or poor inhibition by MgCl2, MnCl, BaCl2, CaCl2, SrCl2, NiCl2, CoCl2Al2(SO4), FeSO4, DTT, and EDTA
-
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Arteritis
Arterivirus nsp12 versus the coronavirus nsp16 2'-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins.
Atherosclerosis
DNA hypomethylation and methyltransferase expression in atherosclerotic lesions.
Brain Injuries
DNA methyltransferase contributes to delayed ischemic brain injury.
Brain Ischemia
DNA methyltransferase contributes to delayed ischemic brain injury.
Carcinogenesis
Inhibition of DNA cytosine methyltransferase by chemopreventive selenium compounds, determined by an improved assay for DNA cytosine methyltransferase and DNA cytosine methylation.
Carcinogenesis
Limited up-regulation of DNA methyltransferase in human colon cancer reflecting increased cell proliferation.
Carcinoma
Inhibition of DNA cytosine methyltransferase by chemopreventive selenium compounds, determined by an improved assay for DNA cytosine methyltransferase and DNA cytosine methylation.
Carcinoma
Limited up-regulation of DNA methyltransferase in human colon cancer reflecting increased cell proliferation.
Colonic Neoplasms
Increased DNA methyltransferase expression is associated with an early stage of human hepatocarcinogenesis.
Colonic Neoplasms
Limited up-regulation of DNA methyltransferase in human colon cancer reflecting increased cell proliferation.
Colonic Neoplasms
Mechanisms for the involvement of DNA methylation in colon carcinogenesis.
Colorectal Neoplasms
Limited up-regulation of DNA methyltransferase in human colon cancer reflecting increased cell proliferation.
COVID-19
In-Silico Drug Designing of Spike Receptor with Its ACE2 Receptor and Nsp10/Nsp16 MTase Complex Against SARS-CoV-2.
Decompression Sickness
Angle and locus of the bend induced by the msp I DNA methyltransferase in a sequence-specific complex with DNA.
Dehydration
Rice cytosine DNA methyltransferases - gene expression profiling during reproductive development and abiotic stress.
Dengue
A structural view of the RNA-dependent RNA polymerases from the Flavivirus genus.
Dengue
An interaction between the methyltransferase and RNA dependent RNA polymerase domains of the West Nile virus NS5 protein.
Dengue
Analysis of flavivirus NS5 methyltransferase cap binding.
Dengue
Computational analysis of methyl transfer reactions in dengue virus methyltransferase.
Dengue
Detection and quantification of flavivirus NS5 methyl-transferase activities.
Dengue
Evaluating the suitability of RNA intervention mechanism exerted by some flavonoid molecules against dengue virus MTase RNA capping site: a molecular docking, molecular dynamics simulation, and binding free energy study.
Dengue
Inhibitor designing, virtual screening, and docking studies for methyltransferase: A potential target against dengue virus.
Dengue
Small molecule inhibitors that selectively block dengue virus methyltransferase.
Dengue
Structure of the NS5 methyltransferase from Zika virus and implications in inhibitor design.
Dengue
The dengue virus NS5 protein as a target for drug discovery.
Dengue
Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay.
Encephalitis, Japanese
A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replication.
Encephalitis, Japanese
A structural view of the RNA-dependent RNA polymerases from the Flavivirus genus.
Encephalitis, Japanese
Crystal structure of full-length Zika virus NS5 protein reveals a conformation similar to Japanese encephalitis virus NS5.
Glioma
DNA methyltransferase levels and altered CpG methylation in the total genome and in the GSTP1 gene in human glioma cells transfected with sense and antisense DNA methyltransferase cDNA.
Hematologic Neoplasms
Cost-effective screening of DNMT3A coding sequence identifies somatic mutation in pediatric T-cell acute lymphoblastic leukemia.
Hepatitis, Chronic
Increased DNA methyltransferase expression is associated with an early stage of human hepatocarcinogenesis.
Herpes Simplex
Chimeric DNA methyltransferases target DNA methylation to specific DNA sequences and repress expression of target genes.
Infarction, Middle Cerebral Artery
DNA methyltransferase contributes to delayed ischemic brain injury.
Infections
Chimeric DNA methyltransferases target DNA methylation to specific DNA sequences and repress expression of target genes.
Infections
Comparative studies of the phage T2 and T4 DNA (N6-adenine)methyltransferases: amino acid changes that affect catalytic activity.
Infections
In-Silico Drug Designing of Spike Receptor with Its ACE2 Receptor and Nsp10/Nsp16 MTase Complex Against SARS-CoV-2.
Infections
MTase Domain of Dendrolimus punctatus cypovirus VP3 Mediates Virion Attachment and Interacts with Host ALP Protein.
Leukemia, Erythroblastic, Acute
Baculovirus-mediated expression and characterization of the full-length murine DNA methyltransferase.
Leukemia, Myeloid, Acute
Functional Analysis of DNMT3A DNA Methyltransferase Mutations Reported in Patients with Acute Myeloid Leukemia.
Lyme Disease
DNA Methylation by Restriction Modification Systems Affects the Global Transcriptome Profile in Borrelia burgdorferi.
Neoplasms
Chemiluminescence resonance energy transfer biosensing platform for site-specific determination of DNA methylation and assay of DNA methyltransferase activity using exonuclease III-assisted target recycling amplification.
Neoplasms
Cytosine-5 methylation-directed construction of a Au nanoparticle-based nanosensor for simultaneous detection of multiple DNA methyltransferases at the single-molecule level.
Neoplasms
Detection of DNA methyltransferase activity using allosteric molecular beacons.
Neoplasms
DNA hypomethylation and methyltransferase expression in atherosclerotic lesions.
Neoplasms
Elevated expression and altered pattern of activity of DNA methyltransferase in liver tumors of rats fed methyl-deficient diets.
Neoplasms
Expression of T:G mismatch-specific thymidine-DNA glycosylase and DNA methyl transferase genes during development and tumorigenesis.
Neoplasms
Highly sensitive fluorescence assay of DNA methyltransferase activity by methylation-sensitive cleavage-based primer generation exponential isothermal amplification-induced G-quadruplex formation.
Neoplasms
Inhibition of C5-cytosine-DNA-methyltransferases.
Neoplasms
Limited up-regulation of DNA methyltransferase in human colon cancer reflecting increased cell proliferation.
Neoplasms
Mechanisms for the involvement of DNA methylation in colon carcinogenesis.
Neoplasms
Molecular mechanisms of adaptive response to alkylating agents in Escherichia coli and some remarks on O(6)-methylguanine DNA-methyltransferase in other organisms.
Neoplasms
Sensitive detection of DNA methyltransferase using the dendritic rolling circle amplification-induced fluorescence.
Neoplasms
Sensitive surface plasmon resonance detection of methyltransferase activity and screening of its inhibitors amplified by p53 protein bound to methylation-specific ds-DNA consensus sites.
Neoplasms
Signal amplification of graphene oxide combining with restriction endonuclease for site-specific determination of DNA methylation and assay of methyltransferase activity.
Neoplasms
Tumor formation and inactivation of RIZ1, an Rb-binding member of a nuclear protein-methyltransferase superfamily.
Neoplasms
Ultrasensitive and Accurate Assay of Human Methyltransferase Activity at the Single-Cell Level Based on a Single Integrated Magnetic Microprobe.
Prostatic Neoplasms
Going beyond Polycomb: EZH2 functions in prostate cancer.
Rabies
Critical Role of K1685 and K1829 in the Large Protein of Rabies Virus in Viral Pathogenicity and Immune Evasion.
Starvation
Regulation of genes encoding subunits of the trehalose synthase complex in Saccharomyces cerevisiae: novel variations of STRE-mediated transcription control?
Stroke
DNA methyltransferase contributes to delayed ischemic brain injury.
Vaccinia
Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity.
Vaccinia
In silico identification, structure prediction and phylogenetic analysis of the 2'-O-ribose (cap 1) methyltransferase domain in the large structural protein of ssRNA negative-strand viruses.
Vaccinia
Reassignment of specificities of two cap methyltransferase domains in the reovirus lambda 2 protein.
Yellow Fever
Analysis of flavivirus NS5 methyltransferase cap binding.
Yellow Fever
Aptamer Displacement Screen for Flaviviral RNA Methyltransferase Inhibitors.
Zika Virus Infection
Structure-based screening and validation of bioactive compounds as Zika virus methyltransferase (MTase) inhibitors through first-principle density functional theory, classical molecular simulation and QM/MM affinity estimation.
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?
x * 65000, SDS-PAGE
?
-
x * 70000, calculated from amino acid sequence
?
-
x * 70000, calculated from amino acid sequence
-
?
-
x * 60700, wild-type, calculated, x * 61000, wild-type, SDS-PAGE, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 68202, sequence calculation, x * 65237, mass spectrometry
?
x * 67000, recombinant enzyme, SDS-PAGE
?
-
x * 67000, recombinant enzyme, SDS-PAGE
-
?
WP_028494267
x * 112000, SDS-PAGE
?
-
x * 110000, calculation from nucleotide sequence
?
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
?
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 63300, about, sequence calculation
dimer
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
dimer
-
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
-
dimer
DrTS consists of a catalytic (beta/alpha)8 barrel, subdomain B, a C-terminal beta-domain and two TS-unique subdomains, S7 and S8. The C-terminal domain and domain S8 contribute the majority of the dimeric interface, analytical ulatracentrifugation. Enzyme structure comparisons, detailed overview
dimer
2 * 68000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
-
homodimer
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
homodimer
-
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
-
homohexamer
-
6 * 65000, SDS-PAGE
homohexamer
-
6 * 68000, gel filtration
homohexamer
-
6 * 65000, SDS-PAGE
homohexamer
-
6 * 68000, gel filtration
tetramer
-
tetramer
-
4 * 67000, SDS-PAGE
tetramer
-
4 * 67000, SDS-PAGE
-
additional information
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
additional information
-
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
additional information
-
each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase
-
additional information
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
-
additional information
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
additional information
-
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
additional information
-
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
-
additional information
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
additional information
-
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
additional information
-
enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview
-
additional information
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
-
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I150F
site-directed mutagenesis, a residue in subdomain B, constitute part of the active-site pocket, the mutant shows 55% of the isomerase activity and 170% of the hydrolase activity compared to wild-type
N253F
site-directed mutagenesis, the apo structure of the DrTS N253F mutant displays a new open conformation with an empty active site. The structure of the N253F mutant is drastically altered compared with that of the wild-type DrTS-Tris complex
Y213A/E320A/E324A
site-directed mutagenesis, the catalytic triad residues, no isomerase or hydrolase activity detected
I150F
-
site-directed mutagenesis, a residue in subdomain B, constitute part of the active-site pocket, the mutant shows 55% of the isomerase activity and 170% of the hydrolase activity compared to wild-type
-
N253A
-
site-directed mutagenesis, residue Asn253 forms a hydrogen bond with Glu324, N253A causes movement of the Glu324 side chain, leading to the creation of a small pore for water entry, the mutant shows 11% of the isomerase activity and 180% of the hydrolase activity compared to wild-type
-
N253F
-
site-directed mutagenesis, the apo structure of the DrTS N253F mutant displays a new open conformation with an empty active site. The structure of the N253F mutant is drastically altered compared with that of the wild-type DrTS-Tris complex
-
R148A
-
site-directed mutagenesis, Arg148 forms salt bridges with Glu223 and Glu324, the mutant shows 12% of the isomerase activity and 150% of the hydrolase activity compared to wild-type
-
Y213A/E320A/E324A
-
site-directed mutagenesis, the catalytic triad residues, no isomerase or hydrolase activity detected
-
R392A
site-directed mutagenesis, the mutant shows a sharp decrease in activity compared to the wild-type enzyme
R392F
site-directed mutagenesis, the mutation leads to a complete loss in activity
R392A
-
site-directed mutagenesis, the mutant shows a sharp decrease in activity compared to the wild-type enzyme
-
R392F
-
site-directed mutagenesis, the mutation leads to a complete loss in activity
-
A255P
-
2.0% activity compared to the wild type enzyme
D411P
-
3.2% activity compared to the wild type enzyme
D41P
-
99.6% activity compared to the wild type enzyme
E469P
-
50% activity compared to the wild type enzyme
I121P
-
21.3% activity compared to the wild type enzyme
I385P
-
5.1% activity compared to the wild type enzyme
K332P
-
96.7% activity compared to the wild type enzyme
N503P
-
the mutant shows about 39% higher relative activity than that of the wild type at 65°C for 120 min. The trehalose yield of the mutant is 1.3fold higher than that of the wild type with sweet potato starch as substrate at 50°C for 4 h
R523P
-
90.8% activity compared to the wild type enzyme
S439P
-
20.8% activity compared to the wild type enzyme
D112A
-
site-directed mutagenesis, inactive mutant
D294A
-
site-directed mutagenesis, inactive mutant
D403A
-
site-directed mutagenesis, inactive mutant
E338A
-
site-directed mutagenesis, inactive mutant
F115A
-
site-directed mutagenesis, inactive mutant
F223A
-
site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
F255A
-
site-directed mutagenesis, inactive mutant
Q259A
-
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
R535A
-
site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
D112A
-
site-directed mutagenesis, inactive mutant
-
D403A
-
site-directed mutagenesis, inactive mutant
-
E338A
-
site-directed mutagenesis, inactive mutant
-
F115A
-
site-directed mutagenesis, inactive mutant
-
F223A
-
site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
-
synthesis
-
usage of the enzyme in a sugar nucleotide cycling process for synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, coupled reaction of trehalose synthase from Pyrococcus horikoshii with UDP-Glc 4-epimerase from Pyrococcus horikoshii, and several alpha-galactosyltransferases, method development and evaluation, overview
K136T/Y137D/K138N/D139S
mutation resulted in improved trehalose yield compared to that of the wild-type enzyme
H534Y
-
site-directed mutagenesis, the mutant enzyme retains 50% activity after 30 min at 70°C
-
R283G/Y287R/R291G
-
site-directed mutagenesis, the mutant enzyme retains 36% activity after 30 min at 70°C
-
R283G/Y287R/R291G/H534Y
-
site-directed mutagenesis, the mutant enzyme retains 25% activity after 30 min at 70°C
-
E330A
site-directed mutagenesis, residue E330 is vital for product formation, the mutant shows only hydrolase activity but no transglucosidic activity
L116E
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 101% activity with maltose and 74% with sucrose compared to wild-type
L116G
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 17% activity with maltose and 144% with sucrose compared to wild-type
L116M
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 118% activity with maltose and 78% with sucrose compared to wild-type
E330A
-
site-directed mutagenesis, residue E330 is vital for product formation, the mutant shows only hydrolase activity but no transglucosidic activity
-
L116E
-
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 101% activity with maltose and 74% with sucrose compared to wild-type
-
L116G
-
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 17% activity with maltose and 144% with sucrose compared to wild-type
-
L116M
-
site-directed mutagenesis, residue L116 forms bond with H120 and D217, supposedly important for substrate specificity, the mutant shows 118% activity with maltose and 78% with sucrose compared to wild-type
-
synthesis
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use of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa for production of trehalose from starch. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
N253A
site-directed mutagenesis, N253A structure shows a small pore created for water entry, the mutant shows a decrease in isomerase activity by 8-9fold and an increase in hydrolase activity by 1.5-1.8fold
N253A
site-directed mutagenesis, residue Asn253 forms a hydrogen bond with Glu324, N253A causes movement of the Glu324 side chain, leading to the creation of a small pore for water entry, the mutant shows 11% of the isomerase activity and 180% of the hydrolase activity compared to wild-type
R148A
site-directed mutagenesis, Arg148 forms salt bridges with Glu223 and Glu324, the mutant shows 12% of the isomerase activity and 150% of the hydrolase activity compared to wild-type
R148A
site-directed mutagenesis, the mutant shows a decrease in isomerase activity by 8-9fold and an increase in hydrolase activity by 1.5-1.8fold
H534Y
site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 50% of the wild-type activity
H534Y
site-directed mutagenesis, the mutant enzyme retains 50% activity after 30 min at 70°C
R283G/Y287R/R291G
site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 36% of the wild-type activity
R283G/Y287R/R291G
site-directed mutagenesis, the mutant enzyme retains 36% activity after 30 min at 70°C
R283G/Y287R/R291G/H534Y
site-directed mutagenesis, mutation of the metal ion-binding site, the mutant shows 35% of the wild-type activity
R283G/Y287R/R291G/H534Y
site-directed mutagenesis, the mutant enzyme retains 25% activity after 30 min at 70°C
additional information
addition of the C-terminal domain of Thermus thermophilus TtTreS to the Corynebacterium glutamicum enzyme CgTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for CgTreS activity enhancement. The specific activity is slightly improved by linking to the TtTreS-C fragment
additional information
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addition of the C-terminal domain of Thermus thermophilus TtTreS to the Corynebacterium glutamicum enzyme CgTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for CgTreS activity enhancement. The specific activity is slightly improved by linking to the TtTreS-C fragment
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additional information
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fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
addition of the C-terminal domain of TtTreS to the Deinococcus radiodurans enzyme DrTreS leads to great improvement of the thermostability of the cold-active DrTreS
additional information
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addition of the C-terminal domain of TtTreS to the Deinococcus radiodurans enzyme DrTreS leads to great improvement of the thermostability of the cold-active DrTreS
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additional information
construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
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construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
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preparation of cross-linked enzyme aggregates in a water-in-oil emulsion, spherical aggregates of recombinant trehalose synthase are obtained through the emulsion based process, method development and evaluation
additional information
application of TreS is quite limited, due to the difficulty in recovering the enzyme from reaction mixtures and its intolerance and instability under extreme circumstances. In order to overcome these limitations, immobilization of TreS is developed using cross-linked enzyme aggregates (CLEAs), a kind of carrier-free immobilization technology. Immobilization of purified His-tagged enzyme on CLEAs-PEI-PEG particles, preparation and microstructures of CLEAs-PEI-PEG and CLEAs-PEI. Method optimization and evaluation, overview. 25% PEG as aggregates precipitant gives maximum activity recovery (65.4%), usage of glutaraldehyde is best in a ratio of 1:0.5
additional information
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application of TreS is quite limited, due to the difficulty in recovering the enzyme from reaction mixtures and its intolerance and instability under extreme circumstances. In order to overcome these limitations, immobilization of TreS is developed using cross-linked enzyme aggregates (CLEAs), a kind of carrier-free immobilization technology. Immobilization of purified His-tagged enzyme on CLEAs-PEI-PEG particles, preparation and microstructures of CLEAs-PEI-PEG and CLEAs-PEI. Method optimization and evaluation, overview. 25% PEG as aggregates precipitant gives maximum activity recovery (65.4%), usage of glutaraldehyde is best in a ratio of 1:0.5
additional information
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construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
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additional information
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application of TreS is quite limited, due to the difficulty in recovering the enzyme from reaction mixtures and its intolerance and instability under extreme circumstances. In order to overcome these limitations, immobilization of TreS is developed using cross-linked enzyme aggregates (CLEAs), a kind of carrier-free immobilization technology. Immobilization of purified His-tagged enzyme on CLEAs-PEI-PEG particles, preparation and microstructures of CLEAs-PEI-PEG and CLEAs-PEI. Method optimization and evaluation, overview. 25% PEG as aggregates precipitant gives maximum activity recovery (65.4%), usage of glutaraldehyde is best in a ratio of 1:0.5
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additional information
the trehalose synthase gene is fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica strain CLIB724 leading to functional enzyme expression and a trehalose yield reaching 73% under optimal conditions. Thermal and pH stabilities of the cell surface-displayed recombinant enzyme are improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose are directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose. Method optimization and evaluation, overview. The optimal reaction temperature is 5°C higher than that of the free purified enzyme reported previously. As the temperature increases from 20°C to 60°C, the final concentrations of glucose increases from approximately 3 to 12.4 g/l. At 70°C the glucose production is approximately 4.4 g/l, and it is clear that the high temperature inhibits the production of trehalose as well as the hydrolysis reaction. The lyophilized engineered Y. lipolytica cells retain their original activity for 15 days at room temperature and lose only 15% activity after storage for 40 days
additional information
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the trehalose synthase gene is fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica strain CLIB724 leading to functional enzyme expression and a trehalose yield reaching 73% under optimal conditions. Thermal and pH stabilities of the cell surface-displayed recombinant enzyme are improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose are directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose. Method optimization and evaluation, overview. The optimal reaction temperature is 5°C higher than that of the free purified enzyme reported previously. As the temperature increases from 20°C to 60°C, the final concentrations of glucose increases from approximately 3 to 12.4 g/l. At 70°C the glucose production is approximately 4.4 g/l, and it is clear that the high temperature inhibits the production of trehalose as well as the hydrolysis reaction. The lyophilized engineered Y. lipolytica cells retain their original activity for 15 days at room temperature and lose only 15% activity after storage for 40 days
additional information
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the trehalose synthase gene is fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica strain CLIB724 leading to functional enzyme expression and a trehalose yield reaching 73% under optimal conditions. Thermal and pH stabilities of the cell surface-displayed recombinant enzyme are improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose are directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose. Method optimization and evaluation, overview. The optimal reaction temperature is 5°C higher than that of the free purified enzyme reported previously. As the temperature increases from 20°C to 60°C, the final concentrations of glucose increases from approximately 3 to 12.4 g/l. At 70°C the glucose production is approximately 4.4 g/l, and it is clear that the high temperature inhibits the production of trehalose as well as the hydrolysis reaction. The lyophilized engineered Y. lipolytica cells retain their original activity for 15 days at room temperature and lose only 15% activity after storage for 40 days
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additional information
addition of the C-terminal domain of Thermus thermophilus TtTreS to the Pseudomonas putida enzyme PpTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment
additional information
large-scale production of enzyme TreS in Escherichia coli for trehalose production, conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
additional information
safe and reliable process of trehalose production by the recombinant enzyme expressed in Escherichis coli strain BL21(DE3). Vector pET15b-treS shows better plasmid stability and TreS expression, the highest activity, 39866 U/g dry cell weight occurs at a lactose concentration of 4 g/l for 7 h at 27°C in a 5-l fermentor at pH 8.0. The use of 30% w/v high-maltose syrup as a substrate can extend the temperature tolerance of enzyme TreS to 60°C. More than 64% of maltose can be converted into trehalose by adding 200 U of TreS per gram of maltose at 50°C for 24 h. The total sugar content of the trehalose syrup reached 95.0% w/w after separation. The recovery rate of trehalose dehydrate reaches 57.0% after slow cooling, and the purity is 99.0%. Method evaluation, detailed overview
additional information
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safe and reliable process of trehalose production by the recombinant enzyme expressed in Escherichis coli strain BL21(DE3). Vector pET15b-treS shows better plasmid stability and TreS expression, the highest activity, 39866 U/g dry cell weight occurs at a lactose concentration of 4 g/l for 7 h at 27°C in a 5-l fermentor at pH 8.0. The use of 30% w/v high-maltose syrup as a substrate can extend the temperature tolerance of enzyme TreS to 60°C. More than 64% of maltose can be converted into trehalose by adding 200 U of TreS per gram of maltose at 50°C for 24 h. The total sugar content of the trehalose syrup reached 95.0% w/w after separation. The recovery rate of trehalose dehydrate reaches 57.0% after slow cooling, and the purity is 99.0%. Method evaluation, detailed overview
additional information
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large-scale production of enzyme TreS in Escherichia coli for trehalose production, conversion of 59% maltose by the purified recombinant enzyme with about 5.1% D-glucose as by-product
-
additional information
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safe and reliable process of trehalose production by the recombinant enzyme expressed in Escherichis coli strain BL21(DE3). Vector pET15b-treS shows better plasmid stability and TreS expression, the highest activity, 39866 U/g dry cell weight occurs at a lactose concentration of 4 g/l for 7 h at 27°C in a 5-l fermentor at pH 8.0. The use of 30% w/v high-maltose syrup as a substrate can extend the temperature tolerance of enzyme TreS to 60°C. More than 64% of maltose can be converted into trehalose by adding 200 U of TreS per gram of maltose at 50°C for 24 h. The total sugar content of the trehalose syrup reached 95.0% w/w after separation. The recovery rate of trehalose dehydrate reaches 57.0% after slow cooling, and the purity is 99.0%. Method evaluation, detailed overview
-
additional information
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addition of the C-terminal domain of Thermus thermophilus TtTreS to the Pseudomonas putida enzyme PpTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment
-
additional information
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addition of the C-terminal domain of Thermus thermophilus TtTreS to the Streptomyces coelicolor enzyme ScTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment
additional information
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addition of the C-terminal domain of Thermus thermophilus TtTreS to the Streptomyces coelicolor enzyme ScTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment
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additional information
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SpyTag and SpyCatcher can spontaneously and rapidly conjugate to form an irreversible and stable covalent bond. The trehalose synthase (TreS) from Thermomonospora curvata is successfully cyclized after the fusion of a SpyTag to its C-terminus and SpyCatcher to the N-terminus
additional information
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addition of the C-terminal domain of Thermus thermophilus TtTreS to the Thermotoga maritima enzyme TmTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved by linking to the TtTreS-C fragment
additional information
deletion mutant lacking 415 amino acids from C-terminus has a lower thermostability and produces more byproducts than wild-type. Fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
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deletion mutant lacking 415 amino acids from C-terminus has a lower thermostability and produces more byproducts than wild-type. Fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
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construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
construction of two truncated enzymes (DM1 and DM2), which show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose
additional information
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construction of two truncated enzymes (DM1 and DM2), which show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose
additional information
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enzyme expression in Escherichia coli strain Rosetta (DE3) for trehalose production, method optimization to 50°C, pH 9.0, 10 h, 10% maltose solution, and co-expression of molecular chaperones sigma32, GroEL, GroES, DnaK and DnaJ greatly increasing the solubility of the trehalose synthase protein. Addition of Ca2+ and DTT increase the activity by 19% and 41%, respectively
additional information
the C-domain of enzyme TtTreS, TtTreS-C, is fused to four different enzymes from other species, i.e. PpTreS, CgTreS, ScTreS, and TmTreS from Pseudomonas putida NBRC 14164, Corynebacterium glutamicum ATCC 13032, Streptomyces coelicolor ATCC 23899, and Thermotoga maritima MSB8, domain structures, overview. A flexible linker peptide between the TreS enzyme and TtTreS-C is essential for its activity enhancement. The specific activities of the four enzymes are improved by linking to the TtTreS-C fragment. When added with the C-terminal domain of TtTreS, the thermostability of a cold-active TreS from Deinococcus radiodurans (DrTreS) is greatly improved
additional information
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the C-domain of enzyme TtTreS, TtTreS-C, is fused to four different enzymes from other species, i.e. PpTreS, CgTreS, ScTreS, and TmTreS from Pseudomonas putida NBRC 14164, Corynebacterium glutamicum ATCC 13032, Streptomyces coelicolor ATCC 23899, and Thermotoga maritima MSB8, domain structures, overview. A flexible linker peptide between the TreS enzyme and TtTreS-C is essential for its activity enhancement. The specific activities of the four enzymes are improved by linking to the TtTreS-C fragment. When added with the C-terminal domain of TtTreS, the thermostability of a cold-active TreS from Deinococcus radiodurans (DrTreS) is greatly improved
additional information
the crude TtTreS is immobilized on the surface of glutaraldehyde-3-aminopropyltriethoxysilane-silicalite-1 (GA-APS-silicalite-1, silicalite-1 modified sequentially with 3-aminopropyltriethoxysilane and glutaraldehyde) without enzyme purification. In this case, a nucleophilic attack takes place at the aldehyde group of glutaraldehyde by the amino group of the protein to form a Schiff base. Preparation of activated silicalite-1, APS-silicalite-1, and GA-APS-silicalite-1 and enzyme immobilization, method optimization, overview. Immobilization also provides TtTreS with potential application in a relatively wide range of temperatures from 40°C to 70°C. The trehalose yield of immobilized TtTreS in first cycle reaches 61.52%. After 22 cycles of enzymatic reaction, the immobilized TtTreS still retains 81% of its initial trehalose yield
additional information
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construction of two truncated enzymes (DM1 and DM2), which show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose
-
additional information
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construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
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medicine
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trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal. The alpha-Gal epitope III with galactulose acceptor shows the most inhibitory activity of anti-adhesion of Escherichia coli cells to human Caco-2 cells. The alpha-galactosyl oligosaccharides may be alternative anti-adhesion molecules that overcome antibiotic resistance
synthesis
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immobilization of recombinant enzyme on Eupergit C250L for the production of trehalose. Immobilization does not affect optimum pH value, optimum temperature is shifted from 45°C to 65°C. Immobilized enzyme is stable at 70°C for 16 days and can be used more than 10times in batch reaction. A maximum yield of 42% trehalose can be reached from 50 g/l maltose
synthesis
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the enzyme is a good candidate in the large-scale production of trehalose from maltose
synthesis
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the enzyme is useful in the biotransformation process for inexpensive production of trehalose from maltose
synthesis
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trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, method development and evaluation, overview
synthesis
WP_028494267
good application potential of the recombinant enzyme in the efficient conversion of trehalose from maltose
synthesis
the enzyme (TreS) produced from Acidiplasma spMBA-1 can catalyze a considerable amount of maltose into trehalose in a single step reaction. Maltose is a relatively cheap substrate. Hence, TreS can be used as an alternative commercial enzyme to produce trehalose commercially. A significant amount of glucose is being produced as a byproduct which hinders the production of commercial trehalose. If it is possible to suppress glucose production by genetic modifications, it could enhance trehalose production
additional information
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physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose was found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose was found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
-
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Thermomonospora curvata
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2017
Thermus thermophilus
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Liu, H.; Yang, S.; Liu, Q.; Wang, R.; Wang, T.
A process for production of trehalose by recombinant trehalose synthase and its purification
Enzyme Microb. Technol.
113
83-90
2018
Pseudomonas putida (Q88FN0), Pseudomonas putida, Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440 (Q88FN0)
brenda
Cho, C.B.; Park, D.Y.; Lee, S.B.
Effect of C-terminal domain truncation of Thermus thermophilus trehalose synthase on its substrate specificity
Enzyme Microb. Technol.
96
121-126
2017
Thermus thermophilus (Q7WUI5), Thermus thermophilus, Thermus thermophilus ATCC 33923 (Q7WUI5)
brenda
Li, N.; Wang, H.; Li, L.; Cheng, H.; Liu, D.; Cheng, H.; Deng, Z.
Integrated approach to producing high-purity trehalose from maltose by the yeast Yarrowia lipolytica displaying trehalose synthase (TreS) on the cell surface
J. Agric. Food Chem.
64
6179-6187
2016
Picrophilus torridus (Q6L2Z7), Picrophilus torridus, Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 (Q6L2Z7)
brenda
Wang, J.; Ren, X.; Wang, R.; Su, J.; Wang, F.
Structural characteristics and function of a new kind of thermostable trehalose synthase from Thermobaculum terrenum
J. Agric. Food Chem.
65
7726-7735
2017
Thermobaculum terrenum (D1CE96), Thermobaculum terrenum, Thermobaculum terrenum ATCC BAA-798 / YNP1 (D1CE96)
brenda
Wang, T.; Dai, K.; Liu, H.; Jia, S.; Wang, R.
Cloning and expression of a trehalose synthase from Pseudomonas putida KT2440 in Bacillus subtilis W800N for the production of trehalose
J. Pure Appl. Microbiol.
8
1687-1692
2014
Pseudomonas putida (Q88FN0), Pseudomonas putida ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440 (Q88FN0)
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brenda
Sun, J.; Wang, S.; Li, W.; Li, R.; Chen, S.; Ri, H.; Kim, T.; Kang, M.; Sun, L.; Sun, X.; Yuan, Q.
Improvement of trehalose production by immobilized trehalose synthase from Thermus thermophilus HB27
Molecules
23
pii: E1087
2018
Thermus thermophilus (O06458)
brenda
Dong, Y.; Ma, L.; Duan, Y.
The effect of high pressure on the intracellular trehalose synthase activity of Thermus aquaticus
World J. Microbiol. Biotechnol.
32
11
2016
Thermus aquaticus, Thermus aquaticus SQ-11
brenda
Cai, X.; Seitl, I.; Mu, W.; Zhang, T.; Stressler, T.; Fischer, L.; Jiang, B.
Combination of sequence-based and in silico screening to identify novel trehalose synthases
Enzyme Microb. Technol.
115
62-72
2018
Micrococcus terreus (A0A1I7MT66), Micrococcus terreus, Thermobaculum terrenum (D1CE96), Thermobaculum terrenum
brenda
Ren, X.; Wang, J.; Li, Y.; Wang, F.; Wang, R.; Li, P.; Ma, C.; Su, J.
Computational and enzymatic analyses unveil the catalytic mechanism of thermostable trehalose synthase and suggest strategies for improved bioconversion
J. Agric. Food Chem.
67
8177-8185
2019
Thermobaculum terrenum (D1CE96), Thermobaculum terrenum
brenda
Kermani, A.; Roy, R.; Gopalasingam, C.; Kocurek, K.; Patel, T.; Alderwick, L.; Besra, G.; Ftterer, K.
Crystal structure of the TreS Pep2 complex, initiating a-glucan synthesis in the GlgE pathway of mycobacteria
J. Biol. Chem.
294
7348-7359
2019
Mycolicibacterium smegmatis (A0R6E0), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R6E0)
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), Thermus antranikianii
brenda
Al Faik, M.; Das, R.; Bo, J.; Mu, W.; Hassanin, H.
Cloning, purification and characterization of a novel recombinant trehalose synthase (TreS) from Acidiplasma sp. MBA-1
J. Microbiol. Biotechnol. Food Sci.
8
1298-1302
2019
Acidiplasma sp. MBA-1 (A0A0D8DNG2)
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brenda
Li, Y.; Gu, Z.; Zhang, L.; Ding, Z.; Shi, G.
Inducible expression of trehalose synthase in Bacillus licheniformis
Protein Expr. Purif.
130
115-122
2017
Thermomonospora curvata (D1ABU6), Thermomonospora curvata, Thermomonospora curvata ATCC 19995 (D1ABU6)
brenda