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4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
alpha-maltotriosyl trehalose
maltopentaose
-
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
maltohexaose
alpha-maltotetraosyl trehalose
maltohexaose
alpha-maltotetraosyltrehalose
maltohexaose
trehalosylmaltotetraose
Maltopentaose
alpha-Maltotriosyl trehalose
maltopentaose
alpha-maltotriosyltrehalose
maltotetraose
alpha-maltosyl trehalose
ratio of transglycosylation to hydrolysis is 38:0.6, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltotetraose
alpha-maltosyltrehalose
maltotriose
alpha-glucosyltrehalose
Short chain amylose
?
-
43% of the activity with maltopentaose
-
-
?
soluble starch
trehalose
-
-
-
-
?
additional information
?
-
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
-
-
-
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
-
-
-
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
-
-
-
?
4-[(1->4)-alpha-D-glucosyl]n-1-D-glucose
1-alpha-D-[(1->4)-alpha-D-glucosyl]n-1-alpha-D-glucopyranoside
-
-
-
?
acarbose
?
-
-
-
-
?
dextrin
?
-
the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
-
-
?
dextrin
?
-
the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
-
-
?
liquified corn starch
?
-
-
in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
-
?
liquified corn starch
?
-
-
in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
-
?
Maltoheptaose
?
-
58% of the activity with maltopentaose
-
-
?
Maltoheptaose
?
-
58% of the activity with maltopentaose
-
-
?
Maltoheptaose
?
-
92% of the activity with maltopentaose
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
-
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
preferred substrate
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
preferred substrate, ratio of transglycosylation to hydrolysis is 100:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
88.6% of the activity compared to maltopentaose
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
88.6% of the activity compared to maltopentaose
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
-
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
-
preferred substrate
-
-
?
maltoheptaose
alpha-maltopentaosyl trehalose
preferred substrate, ratio of transglycosylation to hydrolysis is 100:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltohexaose
?
-
45% of the activity with maltopentaose
-
-
?
Maltohexaose
?
-
45% of the activity with maltopentaose
-
-
?
Maltohexaose
?
-
145% of the activity with maltopentaose
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
EF433294
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
preferred substrate
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
ratio of transglycosylation to hydrolysis is 90:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltohexaose
alpha-maltotetraosyl trehalose
-
preferred substrate
-
-
?
maltohexaose
alpha-maltotetraosyl trehalose
ratio of transglycosylation to hydrolysis is 90:0.2, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltohexaose
alpha-maltotetraosyltrehalose
-
-
-
-
?
maltohexaose
alpha-maltotetraosyltrehalose
-
80% of the activity compared to maltopentaose
-
-
?
maltohexaose
alpha-maltotetraosyltrehalose
-
80% of the activity compared to maltopentaose
-
-
?
maltohexaose
alpha-maltotetraosyltrehalose
-
-
-
-
?
maltohexaose
trehalosylmaltotetraose
-
-
-
-
?
maltohexaose
trehalosylmaltotetraose
-
-
-
-
?
maltopentaose
?
-
-
-
?
maltopentaose
?
-
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
ratio of transglycosylation to hydrolysis is 77:0.6, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
the enzyme also cytalyzes the hydrolysis of maltopentaose
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
the enzyme also cytalyzes the hydrolysis of maltopentaose
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
ratio of transglycosylation to hydrolysis is 77:0.6, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
Maltopentaose
alpha-Maltotriosyl trehalose
-
-
-
-
?
maltopentaose
alpha-maltotriosyltrehalose
-
-
-
-
?
maltopentaose
alpha-maltotriosyltrehalose
-
-
-
-
?
Maltotetraose
?
-
25% of the activity with maltopentaose
-
-
?
Maltotetraose
?
-
25% of the activity with maltopentaose
-
-
?
Maltotetraose
?
-
-
-
-
?
Maltotetraose
?
-
23% of the activity with maltopentaose
-
-
?
maltotetraose
alpha-maltosyltrehalose
-
-
-
-
?
maltotetraose
alpha-maltosyltrehalose
-
46.3% of the activity compared to maltopentaose
-
-
?
maltotetraose
alpha-maltosyltrehalose
-
46.3% of the activity compared to maltopentaose
-
-
?
maltotetraose
alpha-maltosyltrehalose
-
-
-
-
?
maltotriose
alpha-glucosyltrehalose
-
-
-
-
?
maltotriose
alpha-glucosyltrehalose
ratio of transglycosylation to hydrolysis is 10:1.4, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
maltotriose
alpha-glucosyltrehalose
-
5.0% of the activity compared to maltopentaose
-
-
?
maltotriose
alpha-glucosyltrehalose
-
5.0% of the activity compared to maltopentaose
-
-
?
maltotriose
alpha-glucosyltrehalose
ratio of transglycosylation to hydrolysis is 10:1.4, recombinant enzyme
i.e. alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->1)-alpha-D-Glcp
-
?
soluble starch
?
-
-
in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
-
?
soluble starch
?
-
-
in presence of maltooligosyltrehalose trehalohydrolase, conversion of soluble starch into trehalose
-
?
starch
?
-
the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
-
-
?
starch
?
-
the enzyme transforms starch and dextrins to the corresponding trehalosyl derivatives with an intramolecular transglycosylation process that converts the glucosidic linkage at the reducing end from alpha-1,4 to alpha-1,1
-
-
?
additional information
?
-
-
no reaction with maltose
-
-
?
additional information
?
-
-
no reaction with maltose
-
-
?
additional information
?
-
-
the enzyme converts maltooligosaccharides into maltooligosyltrehalose
-
-
?
additional information
?
-
-
enzyme is involved in the pathway of trehalose synthesis from starch
-
-
?
additional information
?
-
-
starch, amylose and amylopectin are no good substrates, MTS is not active on maltotriose
-
-
?
additional information
?
-
-
no activity with maltose. The enzyme never produces a glycosyltrehalose of longer chain length than the substrate used. Glucose and maltooligosaccharide shortened by one glucose residue are produced as by-products
-
-
?
additional information
?
-
-
key enzyme in the synthesis of trehalose
-
-
?
additional information
?
-
key enzyme in the synthesis of trehalose
-
-
?
additional information
?
-
mainly catalyzes an intramolecular transglycosyl reaction to form trehalosyl dextrins from dextrins by converting the alpha-1,4-glucosidic linkage at the reducing end to an alpha-1,1-glucosidic linkage
-
-
?
additional information
?
-
-
no activity with maltose. The enzyme never produces a glycosyltrehalose of longer chain length than the substrate used. Glucose and maltooligosaccharide shortened by one glucose residue are produced as by-products
-
-
?
additional information
?
-
-
enzyme is involved in the pathway of trehalose synthesis from starch
-
-
?
additional information
?
-
-
starch, amylose and amylopectin are no good substrates, MTS is not active on maltotriose
-
-
?
additional information
?
-
key enzyme in the synthesis of trehalose
-
-
?
additional information
?
-
mainly catalyzes an intramolecular transglycosyl reaction to form trehalosyl dextrins from dextrins by converting the alpha-1,4-glucosidic linkage at the reducing end to an alpha-1,1-glucosidic linkage
-
-
?
additional information
?
-
-
possible mechanism of action: after converting the alpha-1,4-glucosidic linkage to an alpha-1,1-glucosidic linkage at the reducing end of maltooligosaccharide Glc(n) is able to release glucose and maltooligosaccharide Glc(n-1) residues. Then the intramolecular transglycosylation and the hydrolytic reaction continues with maltooligosaccharide Glc(n-1) until the initial maltooligosaccharide is reduced to maltose
-
?
additional information
?
-
-
enzyme of trehalose biosynthesis
-
-
?
additional information
?
-
-
MTSase catalyzes the transglycosylation of the reducing-end maltose alpha-1,4-glucosidic bond of its oligosaccharide substrate to a trehalose alpha-1,1-glucosidic bond
-
-
?
additional information
?
-
the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
-
-
?
additional information
?
-
-
the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
-
-
?
additional information
?
-
the archaeal enzyme catalyzes an intramolecular transglycosylation reaction and converts the glycosidic bond at the reducing end of dextrins from alpha-1,4 (reducing end) into alpha-1,1 (non-reducing end). Maltodextrin and maltooligosaccharide are used as substrates by the enzyme but maltose, chitooligosaccharide, sucrose and beta-cyclodextrin are no substrates
-
-
?
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11.6 - 41.5
maltotetraose
228
maltotriose
-
pH 5.5, 60°C
0.6
short chain amylose
-
-
-
additional information
additional information
-
0.9
maltoheptaose
-
-
1.2
maltoheptaose
-
pH 5.5, 60°C
2.84
maltoheptaose
-
mutant F405S, pH 5.0, 60°C
3.38
maltoheptaose
-
mutant F405M, pH 5.0, 60°C
3.8
maltoheptaose
-
mutant F405Y, pH 5.0, 60°C
3.8
maltoheptaose
-
mutant Y409F, pH 5.0, 60°C
3.88
maltoheptaose
-
wild-type, pH 5.0, 60°C
5.71
maltoheptaose
-
mutant F405W, pH 5.0, 60°C
1.4
maltohexaose
-
-
1.4
maltohexaose
-
maltoheptaose
1.87
maltohexaose
EF433294
recombinant enzyme, in 50 mM phosphate-citric acid buffer (0.2 M Na3PO4, 0.1 M citric acid, pH 7.0) at 50°C
1.93
maltohexaose
-
mutant F206W, pH 5.0, 60°C
2
maltohexaose
-
pH 5.5, 75°C
2.48
maltohexaose
-
mutant F206Y, pH 5.0, 60°C
2.7
maltohexaose
-
pH 5.5, 60°C
2.92
maltohexaose
-
mutant F207Y, pH 5.0, 60°C
3.7 - 5
maltohexaose
-
mutant F405S, pH 5.0, 60°C
3.78
maltohexaose
-
mutant Y367F, pH 5.0, 60°C
4.53
maltohexaose
-
wild-type, pH 5.0, 60°C
4.63
maltohexaose
-
mutant F405M, pH 5.0, 60°C
4.9
maltohexaose
-
mutant F405Y, pH 5.0, 60°C
5.9
maltohexaose
-
mutant F405W, pH 5.0, 60°C
6.26
maltohexaose
-
mutant Y409F, pH 5.0, 60°C
26.5
maltohexaose
-
mutant Y290F, pH 5.0, 60°C
5
maltopentaose
-
pH 5.5, 60°C
5.85
maltopentaose
-
mutant Y409F, pH 5.0, 60°C
5.94
maltopentaose
-
wild-type, pH 5.0, 60°C
6.34
maltopentaose
-
mutant F405Y, pH 5.0, 60°C
6.6
maltopentaose
-
mutant F405M, pH 5.0, 60°C
6.6
maltopentaose
pH 5, 60°C, wild-type enzyme
6.6
maltopentaose
pH 5.0, 60°C, wild-type enzyme
7.9
maltopentaose
-
mutant F405W, pH 5.0, 60°C
9.25
maltopentaose
-
mutant F405S, pH 5.0, 60°C
9.74
maltopentaose
pH 5.0, 60°C, mutant enzyme P402Q
10.1
maltopentaose
pH 5.0, 60°C, mutant enzyme A406S
12.6
maltopentaose
pH 5.0, 60°C, mutant enzyme V426T
43.2
maltopentaose
pH 5, 60°C, mutant enzyme D411A
43.2
maltopentaose
pH 5.0, 60°C, mutant enzyme D411A
43.5
maltopentaose
pH 5, 60°C, mutant enzyme R614A
43.5
maltopentaose
pH 5.0, 60°C, mutant enzyme R614A
122
maltopentaose
pH 5, 60°C, mutant enzyme D610A
122
maltopentaose
pH 5.0, 60°C, mutant enzyme D610A
11.6
maltotetraose
-
mutant F405Y, pH 5.0, 60°C
13.2
maltotetraose
-
wild-type, pH 5.0, 60°C
16.1
maltotetraose
-
mutant Y409F, pH 5.0, 60°C
19
maltotetraose
-
mutant F405M, pH 5.0, 60°C
20.2
maltotetraose
-
mutant F405S, pH 5.0, 60°C
20.6
maltotetraose
-
mutant F405W, pH 5.0, 60°C
21.8
maltotetraose
-
pH 5.5, 60°C
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
147
maltoheptaose
-
mutant F405S, pH 5.0, 60°C
282
maltoheptaose
-
mutant Y409F, pH 5.0, 60°C
363
maltoheptaose
-
mutant F405Y, pH 5.0, 60°C
381
maltoheptaose
-
mutant F405M, pH 5.0, 60°C
383
maltoheptaose
-
wild-type, pH 5.0, 60°C
429
maltoheptaose
-
mutant F405W, pH 5.0, 60°C
6.11
maltohexaose
-
mutant F206Y, pH 5.0, 60°C
11.1
maltohexaose
-
mutant F206W, pH 5.0, 60°C
14
maltohexaose
-
mutant F207Y, pH 5.0, 60°C
26.5
maltohexaose
-
mutant Y290F, pH 5.0, 60°C
33
maltohexaose
-
pH 5.5, 75°C
139
maltohexaose
-
mutant Y367F, pH 5.0, 60°C
169
maltohexaose
-
mutant F405S, pH 5.0, 60°C
330
maltohexaose
-
mutant Y409F, pH 5.0, 60°C
359
maltohexaose
-
wild-type, pH 5.0, 60°C
362
maltohexaose
-
mutant F405Y, pH 5.0, 60°C
414
maltohexaose
-
mutant F405M, pH 5.0, 60°C
445
maltohexaose
-
mutant F405W, pH 5.0, 60°C
13.4
maltopentaose
pH 5, 60°C, mutant enzyme R614A
13.4
maltopentaose
pH 5.0, 60°C, mutant enzyme R614A
30.2
maltopentaose
pH 5, 60°C, mutant enzyme D411A
30.2
maltopentaose
pH 5.0, 60°C, mutant enzyme D411A
87.2
maltopentaose
pH 5, 60°C, mutant enzyme D610A
87.2
maltopentaose
pH 5.0, 60°C, mutant enzyme D610A
197
maltopentaose
-
mutant F405S, pH 5.0, 60°C
267
maltopentaose
-
mutant Y409F, pH 5.0, 60°C
280
maltopentaose
pH 5.0, 60°C, mutant enzyme P402Q
354
maltopentaose
-
mutant F405Y, pH 5.0, 60°C
357
maltopentaose
pH 5.0, 60°C, mutant enzyme V426T
364
maltopentaose
-
wild-type, pH 5.0, 60°C
410
maltopentaose
-
mutant F405W, pH 5.0, 60°C
411
maltopentaose
pH 5, 60°C, wild-type enzyme
411
maltopentaose
pH 5.0, 60°C, wild-type enzyme
481
maltopentaose
-
mutant F405M, pH 5.0, 60°C
530
maltopentaose
pH 5.0, 60°C, mutant enzyme A406S
61
maltotetraose
-
mutant F405S, pH 5.0, 60°C
114
maltotetraose
-
mutant Y409F, pH 5.0, 60°C
138
maltotetraose
-
wild-type, pH 5.0, 60°C
139
maltotetraose
-
mutant F405W, pH 5.0, 60°C
139
maltotetraose
-
mutant F405Y, pH 5.0, 60°C
196
maltotetraose
-
mutant F405M, pH 5.0, 60°C
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up
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enzyme expression, as well as accumulations of both trehalose and especially sucrose in filaments, are upregulated significantly under dehydration stress, NaCl stress, and high temperature-drought stress
A406
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly increased
A406S
the hydrolysis/transglycosylation selectivity ratio shows little change
F206W
-
significant decrease in transglycosylation activity
F206Y
-
significant decrease in transglycosylation activity
F207Y
-
significant decrease in transglycosylation activity
F405M
-
catalytic activity comparable to wild-type
F405S
-
depending on substrate, 29-97% of wild-type transglycosylation efficiency, hydrolytic activity is 16% of wild-type
F405W
-
catalytic activity slightly lower than wild-type
P402
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly decreased
P402Q
the hydrolysis/transglycosylation selectivity ratio is significantly decreased
V426
little change in hydrolysis:transglycosylation selectivity ratio
Y290F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis and transglycosylation reaction are 6.6 and 5.6% resp., of wild-type
Y367F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis and transglycosylation reaction are about half of wild-type
Y409F
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for hydrolysis is similar to wild-type, for transglycosylation reaction somewhat lower than wild-type
A406S
-
the hydrolysis/transglycosylation selectivity ratio shows little change
-
D411A
-
significant reductions in catalytic efficiency and increase in the transition-state energy
-
D610A
-
significant reductions in catalytic efficiency and increase in the transition-state energy
-
P402Q
-
the hydrolysis/transglycosylation selectivity ratio is significantly decreased
-
R614A
-
significant reductions in catalytic efficiency and increase in the transition-state energy
-
A406
-
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly increased
-
D610A
-
significant reductions in catalytic efficiency, increase in the transition-state energy
-
P402
-
compared with wild-type enzyme, the hydrolysis:transglycosylation selectivity ratio is significantly decreased
-
R614A
-
significant reductions in catalytic efficiency, increase in the transition-state energy
-
V426
-
little change in hydrolysis:transglycosylation selectivity ratio
-
D228N
-
complete loss of both hydrolytic and transglycosylation activity
D231A
-
significant decrease of both hydrolytic and transglycosylation activity
D275A
-
about 50% and 40% decrease of hydrolytic and transglycosylation activity, resp.
D394A
-
significant decrease of both hydrolytic and transglycosylation activity
D443N
-
complete loss of both hydrolytic and transglycosylation activity
E255Q
-
complete loss of both hydrolytic and transglycosylation activity
E393A
-
complete loss of both hydrolytic and transglycosylation activity
H229N
-
complete loss of both hydrolytic and transglycosylation activity
K256T
-
significant decrease of both hydrolytic and transglycosylation activity
K390A
-
increase in hydrolytic, decrease in transglycosylation activity
K390E
-
increase in hydrolytic, decrease in transglycosylation activity
K390H
-
increase in hydrolytic, decrease in transglycosylation activity
K390Q
-
increase in hydrolytic, decrease in transglycosylation activity
K390R
-
increase in hydrolytic, decrease in transglycosylation activity
K390W
-
complete loss of transglycosylation activity, increase in hydrolytic activity
K390W/K445W
-
complete loss of transglycosylation activity, 40% decrease in hydrolytic activity
K445A
-
increase in hydrolytic, decrease in transglycosylation activity
K445E
-
increase in hydrolytic, decrease in transglycosylation activity
K445H
-
increase in hydrolytic, decrease in transglycosylation activity
K445Q
-
increase in hydrolytic, decrease in transglycosylation activity
K445R
-
increase in hydrolytic, decrease in transglycosylation activity
K445T
-
increase in hydrolytic, significant decrease in transglycosylation activity
K445W
-
complete loss of transglycosylation activity, increase in hydrolytic activity
R192A
-
about 50% and 40% decrease of hydrolytic and transglycosylation activity, resp.
R402S
-
about 30% decrease of both hydrolytic and transglycosylation activity
Y274S
-
significant decrease of both hydrolytic and transglycosylation activity
Y400S
-
about 25% and 20% decrease of hydrolytic and transglycosylation activity, resp.
D411A
significant reductions in catalytic efficiency, increase in the transition-state energy
D411A
significant reductions in catalytic efficiency and increase in the transition-state energy
D610A
significant reductions in catalytic efficiency, increase in the transition-state energy
D610A
significant reductions in catalytic efficiency and increase in the transition-state energy
F405Y
-
decreased ratio of hydrolysis to transglycosylation
F405Y
-
mutation located near subsite +1 constructed to alter enzyme selectivity. Catalytic efficiency for transglycosylation reaction is similar to wild-type, for hydrolysis somewhat lower than wild-type
R614A
significant reductions in catalytic efficiency, increase in the transition-state energy
R614A
significant reductions in catalytic efficiency and increase in the transition-state energy
K390T
-
increase in hydrolytic, decrease in transglycosylation activity
K390T
-
increase in hydrolytic, significant decrease in transglycosylation activity
additional information
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overexpression of BvMTSH, a fusion gene for maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase, enhances drought tolerance in transgenic Oryza sativa without growth inhibition. The transgenic pants show an abscisic acid-hyposensitive phenotype in the roots, phenotype, overview. Construction of the bifunctional in-frame fusion of maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase from the nonpathogenic bacterium Brevibacterium helvolum under the control of the constitutive rice cytochrome c promoter (101MTSH) or the ABA-inducible Ai promoter (105MTSH). BvMTS converts maltooligosaccharides into maltooligosyltrehalose and BvMTH releases trehalose
additional information
comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris strain KM71 and Escherichia coli strain BL21(DE3) for enzyme production. Comparison of the effect of different promoters on MTSase expression in Pichia pastoris, two different expression vectors are investigated: pPIC3.5 K, which contains an inducible alcohol oxidase (AOX1) promoter, and pGAPZA, which contains a constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. The optimal pH, optimal temperature, pH stability, and temperature stability of MTSase expressed in different hosts are investigated and compared, overview. Both of the recombinant enzymes meet the demands of industrial trehalose production with respect to temperature stability
additional information
-
comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris strain KM71 and Escherichia coli strain BL21(DE3) for enzyme production. Comparison of the effect of different promoters on MTSase expression in Pichia pastoris, two different expression vectors are investigated: pPIC3.5 K, which contains an inducible alcohol oxidase (AOX1) promoter, and pGAPZA, which contains a constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. The optimal pH, optimal temperature, pH stability, and temperature stability of MTSase expressed in different hosts are investigated and compared, overview. Both of the recombinant enzymes meet the demands of industrial trehalose production with respect to temperature stability
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Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius
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Sulfolobus acidocaldarius
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brenda
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Acta Crystallogr. Sect. D
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Sulfolobus acidocaldarius
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Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius
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Sulfolobus acidocaldarius
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Metabolic engineering of Corynebacterium glutamicum for trehalose overproduction: role of the TreYZ trehalose biosynthetic pathway
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72
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Corynebacterium glutamicum
brenda
Streeter, J.G.; Gomez, M.L.
Three enzymes for trehalose synthesis in Bradyrhizobium cultured bacteria and in bacteroids from soybean nodules
Appl. Environ. Microbiol.
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Bradyrhizobium japonicum, Bradyrhizobium elkanii
brenda
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Mutations on aromatic residues of the active site to alter selectivity of the Sulfolobus solfataricus maltooligosyltrehalose synthase
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Protein engineering of Sulfolobus solfataricus maltooligosyltrehalose synthase to alter its selectivity
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55
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Saccharolobus solfataricus
brenda
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Creation of a novel hydrolase by site-directed mutagenesis of malto-oligosyltrehalose synthase
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53
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2006
Sulfolobus acidocaldarius
-
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Molecular cloning and characterization of trehalose biosynthesis genes from hyperthermophilic archaebacterium Metallosphaera hakonesis
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17
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2007
Metallosphaera hakonensis
brenda
Lee, J.S.; Hai, T.; Pape, H.; Kim, T.J.; Suh, J.W.
Three trehalose synthetic pathways in the acarbose-producing Actinoplanes sp. SN223/29 and evidence for the TreY role in biosynthesis of component C
Appl. Microbiol. Biotechnol.
80
767-778
2008
Actinoplanes sp., Actinoplanes sp. SN223/29
brenda
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Trehalose-producing enzymes MTSase and MTHase in Anabaena 7120 under NaCl stress
Curr. Microbiol.
56
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2008
Anabaena sp., Anabaena sp. 7120
brenda
Fang, T.Y.; Tseng, W.C.; Shih, T.Y.; Wang, M.Y.
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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2008
Saccharolobus solfataricus
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Production of a thermophilic maltooligosyl-trehalose synthase in Lactococcus lactis
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35
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2008
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
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Bifunctional recombinant fusion enzyme between maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase of thermophilic microorganism Metallosphaera hakonensis
J. Microbiol. Biotechnol.
18
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2008
Metallosphaera hakonensis, Metallosphaera hakonensis JCM 8857
brenda
Wu, S.; Shen, R.; Zhang, X.; Wang, Q.
Molecular cloning and characterization of maltooligosyltrehalose synthase gene from Nostoc flagelliforme
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20
579-586
2010
Nostoc flagelliforme (EF433294), Nostoc flagelliforme
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Cielo, C.B.; Okazaki, S.; Suzuki, A.; Mizushima, T.; Masui, R.; Kuramitsu, S.; Yamane, T.
Structure of ST0929, a putative glycosyl transferase from Sulfolobus tokodaii
Acta Crystallogr. Sect. F
66
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2010
Sulfurisphaera tokodaii
brenda
Shuangxiu, W.; He, L.; Shen, R.; Zhang, X.; Wang, Q.
Molecular cloning of maltooligosyltrehalose trehalohydrolase gene from Nostoc flagelliforme and trehalose-related response to stresses
J. Microbiol. Biotechnol.
21
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2011
Nostoc flagelliforme
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Cloning and expression of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius in Escherichia coli
Sheng Wu Gong Cheng Xue Bao
17
339-341
2001
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius ATCC 49426
brenda
Chen, W.; Liu, L.; Sun, P.; Jin, C.
Cloning and expression of the gene encoding maltoologosyl trehalose synthase from Sulfolobus shibatae in E. coli
Wei Sheng Wu Xue Bao
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Saccharolobus shibatae
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Starch
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Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
-
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Identification of substrate-binding and selectivity-related residues of maltooligosyltrehalose synthase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
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56
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Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
Extremophiles
8
335-343
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Saccharolobus solfataricus (Q7LX98), Saccharolobus solfataricus P2 (Q7LX98)
brenda
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Over-expression of BvMTSH, a fusion gene for maltooligosyltrehalose synthase and maltooligosyltrehalose trehalohydrolase, enhances drought tolerance in transgenic rice
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47
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2014
Brevibacterium helvolum
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Extremophiles
2
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1998
Saccharolobus shibatae, Saccharolobus shibatae DMS 5389
brenda
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Cloning, expression and characterization of the maltooligosyl trehalose synthase from the archaeon Sulfolobus tokodaii
Pak. J. Pharm. Sci.
31
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Sulfurisphaera tokodaii (Q973H2), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q973H2)
brenda
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A comparative study of maltooligosyltrehalose synthase from Sulfolobus acidocaldarius expressed in Pichia pastoris and Escherichia coli
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60
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Sulfolobus acidocaldarius (Q53688), Sulfolobus acidocaldarius ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770 (Q53688)
-
brenda