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4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
glucosyl trehalose + H2O
glucose + trehalose
-
-
-
?
maltoheptaosyltrehalose + H2O
maltoheptaose + alpha,alpha'-trehalose
-
-
-
-
?
maltooligosacccharide + H2O
D-glucose
-
-
-
-
?
maltooligosyltrehalose + H2O
maltooligosaccharide + alpha,alpha'-trehalose
maltooligosyltrehalose + H2O
trehalose + ?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
maltosylpentaosyltrehalose + H2O
trehalose + maltopentaose
maltosyltetraosyltrehalose + H2O
trehalose + maltotetraose
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
maltosyltrehalose + H2O
trehalose + maltose
maltosyltriosyltrehalose + H2O
trehalose + maltotriose
maltotetraose + H2O
?
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
maltotriosyltrehalose + H2O
trehalose + maltotriose
-
-
-
?
additional information
?
-
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
enzyme is up-regulated under NaCl stress, starting at about 36 hours of exposure, acts together with maltooligosyltrehalose synthase
-
-
r
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
enzyme is up-regulated under NaCl stress, starting at about 36 hours of exposure, acts together with maltooligosyltrehalose synthase
-
-
r
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
yield of trehalose production is relatively low but may be increased in the presence of alpha-amylase
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
hydrolysis to disaccharides after 24 h
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
yield of trehalose production is relatively low but may be increased in the presence of alpha-amylase
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
hydrolysis to disaccharides after 24 h
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
hydrolysis to disaccharides after 24 h
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
-
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
-
-
-
?
4'-O-(1,4-alpha-D-glucosyl)n-alpha,alpha'-trehalose + H2O
(1,4-alpha-D-glucosyl)n + alpha,alpha'-trehalose
-
with isoamylase and maltooligosyltrehalose synthase
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
for glucose formation, maltohexaose exhibits the highest formation rate
-
-
?
maltooligosyltrehalose + H2O
maltooligosaccharide + alpha,alpha'-trehalose
-
-
-
?
maltooligosyltrehalose + H2O
maltooligosaccharide + alpha,alpha'-trehalose
-
alpha-1,4-glucosidic and alpha-1,1-linked terminal dissaccharides of maltooligosyltrehalose
trehalose
-
?
maltooligosyltrehalose + H2O
trehalose + ?
-
-
-
-
?
maltooligosyltrehalose + H2O
trehalose + ?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
-
-
-
-
?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
-
-
-
-
?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
-
-
-
-
?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
trehalose formation rate increases as the degree of polymerization value of the substrate increases. maltopentaosyl trehalose is the most preferred substrate for trehalose formation
-
-
?
maltopentaosyltrehalose + H2O
maltopentaose + alpha,alpha'-trehalose
-
-
-
-
?
maltosylpentaosyltrehalose + H2O
trehalose + maltopentaose
93.4% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosylpentaosyltrehalose + H2O
trehalose + maltopentaose
93.4% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltetraosyltrehalose + H2O
trehalose + maltotetraose
hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltetraosyltrehalose + H2O
trehalose + maltotetraose
hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
-
-
-
-
?
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
-
-
-
-
?
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
-
-
-
?
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
-
-
-
?
maltosyltrehalose + H2O
trehalose + maltose
14.4% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltrehalose + H2O
trehalose + maltose
14.4% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltriosyltrehalose + H2O
trehalose + maltotriose
91.6% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltosyltriosyltrehalose + H2O
trehalose + maltotriose
91.6% of the activity compared to maltosyltetraosyltrehalose, hydrolyzes glycosyltrehaloses from the side of the reducing end only by cleavage of the alpha-1,4 glucosidic bond adjacent to the alpha-1,1 glucosidic bond to liberate trehalose
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
sequential hydrolysis by the bifunctional fusion enzyme of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH), synthase converts alpha-1,4-glycosidic linkage into alpha-1,1 linkage to produce maltotriosyltrehalose, which is the substrate for the MTH to produce trehalose
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
sequential hydrolysis by the bifunctional fusion enzyme of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH), synthase converts alpha-1,4-glycosidic linkage into alpha-1,1 linkage to produce maltotriosyltrehalose, which is the substrate for the MTH to produce trehalose
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
sequential hydrolysis by the bifunctional fusion enzyme of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH), synthase converts alpha-1,4-glycosidic linkage into alpha-1,1 linkage to produce maltotriosyltrehalose, which is the substrate for the MTH to produce trehalose
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of trehalose from maltooligosaccharides
-
-
?
additional information
?
-
-
the enzyme releases trehalose from maltooligosyltrehalose
-
-
?
additional information
?
-
-
increase in trehalose level during NaCl stress is the result of overexpression of the trehalose-forming enzymes malooligosyltrehalose synthase (EC 5.4.99.15) and maltooligosyltrehalose trehalohydrolase
-
-
?
additional information
?
-
MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview
-
-
?
additional information
?
-
hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview
-
-
?
additional information
?
-
the crystal structure reveals a scheme for substrate recognition that involves two unique interactions: stacking of Tyr325 with the terminal glucose ring of the trehalose moiety and perpendicularly placement of Trp215 to the pyranose rings at the subsites -1 and +1 glucose
-
-
?
additional information
?
-
substrate potato starch in combined reaction with trehalose-producing (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, MTSase (EC 5.4.99.15), recombinant enzyme
-
-
?
additional information
?
-
substrate potato starch in combined reaction with trehalose-producing (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, MTSase (EC 5.4.99.15), recombinant enzyme
-
-
?
additional information
?
-
the crystal structure reveals a scheme for substrate recognition that involves two unique interactions: stacking of Tyr325 with the terminal glucose ring of the trehalose moiety and perpendicularly placement of Trp215 to the pyranose rings at the subsites -1 and +1 glucose
-
-
?
additional information
?
-
MTHase catalyzes the release of trehalose by cleaving the alpha-1,4-glucosidic linkage next to the alpha-1,1-linked terminal disaccharide of maltooligosyltrehalose, D255, E286, and D380 are essential catalytic residues, while residues A259, Y328, F355, and R356 are related to enzyme selectivity, mutational analysis, overview
-
-
?
additional information
?
-
hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview
-
-
?
additional information
?
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose
-
-
?
additional information
?
-
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose
-
-
?
additional information
?
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose. The recombinant MTHase can catalyze the production of trehalose from starch at high yield when coupled with the maltooligosyl trehalose synthase from the same strain
-
-
?
additional information
?
-
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose. The recombinant MTHase can catalyze the production of trehalose from starch at high yield when coupled with the maltooligosyl trehalose synthase from the same strain
-
-
?
additional information
?
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose
-
-
?
additional information
?
-
maltooligosyl trehalose trehalohydrolase (MTHase) catalyzes the release of trehalose by splitting the alpha-1,4-glucosidic linkage adjacent to the alpha-1,1-glucosidic linkage of maltooligosyl trehalose. The recombinant MTHase can catalyze the production of trehalose from starch at high yield when coupled with the maltooligosyl trehalose synthase from the same strain
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
additional information
?
-
the recombinant mutant enzyme is active against starch in combination with enzyme MTSase, EC 5.4.99.15, that produces trehalose from starch
-
-
?
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2.19 - 2.88
maltoheptaose
4.18 - 39.2
maltooligosyltrehalose
5.08 - 7.74
maltopentaose
4.2 - 5.89
maltopentaosyl trehalose
5.26 - 7.15
maltopentaosyltrehalose
5.5 - 16.7
maltosyl trehalose
4.7
maltosylpentaosyltrehalose
pH 5.5, 60°C
5.6
maltosyltetraosyltrehalose
pH 5.5, 60°C
22.4
maltosyltrehalose
pH 5.5, 60°C
5.8
maltosyltriosyltrehalose
pH 5.5, 60°C
3.7 - 7
maltotetraosyl trehalose
5.03 - 7.91
maltotetraosyltrehalose
2.7 - 7.22
maltotriosyl trehalose
7.22 - 13.6
maltotriosyltrehalose
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
2.19
maltoheptaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.19
maltoheptaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.63
maltoheptaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.81
maltoheptaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.88
maltoheptaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.16
maltohexaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
3.01
maltohexaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
3.42
maltohexaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
4.69
maltohexaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
5.63
maltohexaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
20.5
maltohexaose
-
mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
23.2
maltohexaose
-
mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
4.18
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme H195A
5.02
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155F
5.22
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, wild-type enzyme
7.48
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme E450A
10.7
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme R447A
12.9
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme D156A
39.2
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155A
5.08
maltopentaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
5.37
maltopentaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
5.82
maltopentaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
5.86
maltopentaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
7.74
maltopentaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
4.2
maltopentaosyl trehalose
-
-
4.9
maltopentaosyl trehalose
-
-
5.89
maltopentaosyl trehalose
-
5.26
maltopentaosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
5.75
maltopentaosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
5.81
maltopentaosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
5.89
maltopentaosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
7.15
maltopentaosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
5.5
maltosyl trehalose
-
-
11.1
maltosyl trehalose
-
16.7
maltosyl trehalose
-
-
3.7
maltotetraosyl trehalose
-
-
5.66
maltotetraosyl trehalose
-
7
maltotetraosyl trehalose
-
-
5.03
maltotetraosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
5.66
maltotetraosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
6.73
maltotetraosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
6.79
maltotetraosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
6.79
maltotetraosyltrehalose
-
mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
6.94
maltotetraosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
7.91
maltotetraosyltrehalose
-
mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
2.7
maltotriosyl trehalose
-
-
4.6
maltotriosyl trehalose
-
-
7.22
maltotriosyl trehalose
-
7.22
maltotriosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
8.55
maltotriosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
8.9
maltotriosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
10.9
maltotriosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
13.6
maltotriosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.15 - 1070
maltooligosyltrehalose
14.4 - 19.1
maltopentaose
1230
maltopentaosyl trehalose
-
675 - 1282
maltopentaosyltrehalose
1190
maltotetraosyl trehalose
-
16 - 1192
maltotetraosyltrehalose
1030
maltotriosyl trehalose
-
572 - 1030
maltotriosyltrehalose
additional information
maltoheptaose
-
5
maltoheptaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
5.49
maltoheptaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
6.01
maltoheptaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
6.49
maltoheptaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
6.49
maltoheptaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
0.36
maltohexaose
-
mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
0.54
maltohexaose
-
mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
8.23
maltohexaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
9.5
maltohexaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
12.6
maltohexaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
13.5
maltohexaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
18.2
maltohexaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
2.15
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme H195A
27.8
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155F
44.8
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155A
303
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme R447A
608
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme D156A
947
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, wild-type enzyme
1070
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme E450A
14.4
maltopentaose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5
15.5
maltopentaose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
17.4
maltopentaose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
17.7
maltopentaose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
19.1
maltopentaose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation
675
maltopentaosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
741
maltopentaosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
760
maltopentaosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1226
maltopentaosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1282
maltopentaosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
16
maltotetraosyltrehalose
-
mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
58.4
maltotetraosyltrehalose
-
mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
627
maltotetraosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
654
maltotetraosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
721
maltotetraosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1106
maltotetraosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1192
maltotetraosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
572
maltotriosyltrehalose
-
mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
634
maltotriosyltrehalose
-
mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
734
maltotriosyltrehalose
-
mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1002
maltotriosyltrehalose
-
mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
1030
maltotriosyltrehalose
-
wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation
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D156A
-
kcat/Km for maltooligosyltrehalose is 3.8fold lower than wild-type value
D252E
mutant shows 0.03% of enzymatic activity compared to the wild-type
D252S
mutant shows 0.6% of enzymatic activity compared to the wild-type
E283Q
mutant shows 0.04% of enzymatic activity compared to the wild-type
E450A
-
kcat/Km for maltooligosyltrehalose is 1.2fold lower than wild-type value
H195A
-
kcat/Km for maltooligosyltrehalose is 357fold lower than wild-type value
R447A
-
kcat/Km for maltooligosyltrehalose is 6.5fold lower than wild-type value
Y155A
-
kcat/Km for maltooligosyltrehalose is 160fold lower than wild-type value
Y155F
-
kcat/Km for maltooligosyltrehalose is 33fold lower than wild-type value
D156A
-
kcat/Km for maltooligosyltrehalose is 3.8fold lower than wild-type value
-
D252E
-
mutant shows 0.03% of enzymatic activity compared to the wild-type
-
D252S
-
mutant shows 0.6% of enzymatic activity compared to the wild-type
-
E283Q
-
mutant shows 0.04% of enzymatic activity compared to the wild-type
-
E450A
-
kcat/Km for maltooligosyltrehalose is 1.2fold lower than wild-type value
-
H195A
-
kcat/Km for maltooligosyltrehalose is 357fold lower than wild-type value
-
Y155A
-
kcat/Km for maltooligosyltrehalose is 160fold lower than wild-type value
-
Y155F
-
kcat/Km for maltooligosyltrehalose is 33fold lower than wild-type value
-
A259S
-
site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
-
D255A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
-
D380A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
-
E286A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
-
W218A
-
site-directed mutagenesis, the mutant shows decreased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
-
A259S
site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
A259S
-
mutation increases selectivity ratio glucose/trehalose formation
D255A
-
0.15% of wild-type activity
D255A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
D380A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
D380A
-
0.01% of wild-type activity
E286A
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type MTHase
E286A
-
0.09% of wild-type activity
F355Y
site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
F355Y
-
mutation increases selectivity ratio glucose/trehalose formation
R356K
site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
R356K
-
mutation increases selectivity ratio glucose/trehalose formation
W218A
site-directed mutagenesis, the mutant shows decreased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
W218A
-
mutation decreases selectivity ratio glucose/trehalose formation
W218F
site-directed mutagenesis, the mutant shows decreased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
W218F
-
mutation decreases selectivity ratio glucose/trehalose formation
Y328F
site-directed mutagenesis, the mutant shows increased selectivity ratios, i.e. ratios of the catalytic efficiencies for glucose formation to those for trehalose formation in the hydrolysis of maltooligosaccharides and maltooligosyltrehaloses, respectively
Y328F
-
mutation increases selectivity ratio glucose/trehalose formation
additional information
-
introduction of the trehalose biosynthesis pathway without producing trehalose 6-phosphate as an intermediate in plants: construction of a gene that encodes a bifunctional in-frame fusion (BvMTSH) of maltooligosyltrehalose synthase (BvMTS) and maltooligosyltrehalose trehalohydrolase (BvMTH) from the nonpathogenic bacterium Brevibacterium helvolum to avoid growth inhibition by trehalose 6-phosphate in transgenic Oryzsa sativa subsp. japonica cv. Nakdong plants. Transgenic rice plants that overexpress BvMTSH under the control of the constitutive rice cytochrome c promoter (101MTSH) or the abscisic acid-inducible Ai promoter (105MTSH) show enhanced drought tolerance without growth inhibition, as well as an abscisic acid-hyposensitive phenotype in the roots, overview
additional information
-
bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
additional information
-
bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
-
additional information
-
bifunctional fusion enzyme (MhMTSH) of maltooligosyltrehalose synthase (MhMTS) and malooligosyltrehalose trehalohydrolase (MhMTH)
-
additional information
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
additional information
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
additional information
-
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
-
additional information
-
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
-
additional information
-
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
-
additional information
-
generation of a specific deletion mutation, designed on the basis of sequence alignments of the adjacent ORFs and the published Sulfolobus sp. MTHases, allowing soluble expression in Escherichia coli as active acidic and thermophilic enzyme
-
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Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
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Purification and characterization of a novel enzyme, maltooligosyl trehalose trehalohydrolase, from Arthrobacter sp. Q36
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Formation of trehalose from maltooligosaccharides by a novel enzymatic system
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1995
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Novel enzymes, maltooligosyl trehalose synthase and maltooligosyl trehalose trehalohydrolase and their application to the production of trehalose from starch
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1996
Arthrobacter sp.
-
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Production of trehalose from starch by thermostable enzymes from Sulfolobus acidocaldarius
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-
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301
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162
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17
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56
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56
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Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
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Bifunctional recombinant fusion enzyme between maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase of thermophilic microorganism Metallosphaera hakonensis
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Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
-
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37
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Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus ATCC 33909 (Q55088)
-
brenda