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Information on EC 3.2.1.141 - 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q55088
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3.2.1.141 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolaseSpecify your search results
Word Map
- 3.2.1.141
- sulfolobus
- maltooligosaccharides
- disaccharide
- solfataricus
- starch
- mtsases
-
trey
- acidocaldarius
-
arthrobacter
- synthesis
-
amylolytic
-
alpha-1,4-glucosidic
- maltopentaose
-
archaebacterium
- food industry
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
mthase, maltooligosyltrehalose trehalohydrolase, mhmth, gthase, maltooligosyl trehalose trehalohydrolase, bvmth, st0926, glycosyltrehalose trehalohydrolase, stmthase, st0927, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase
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-
-
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malto-oligosyltrehalose trehalohydrolase
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-
-
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Maltooligosyl trehalose trehalohydrolase
maltooligosyl trehalose trehalohydrolase (Rhizobium strain M-11 clone pMBTU1 gene treZ reduced)
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-
-
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maltooligosyltrehalose trehalohydrolase
maltooligosyltrehalose trehalosidase
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MTHase
trehalosidase, maltooligosyltrehalose
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-
-
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trehalosidase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treZ reduced)
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-
-
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Maltooligosyl trehalose trehalohydrolase
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-
-
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maltooligosyltrehalose trehalohydrolase
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-
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MTHase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-[(1->4)-alpha-D-glucano]trehalose glucanohydrolase (trehalose-producing)
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CAS REGISTRY NUMBER
COMMENTARY
170780-50-4
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176431-02-0
trehalosidase, maltooligosyltrehalose (Rhizobium strain M-11 clone pBMTU1 gene treZ reduced) /maltooligosyl trehalose trehalohydrolase (Rhizobium strain M-11 clone pMBTU1 gene treZ reduced)
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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
-
-
?
maltooligosyltrehalose + H2O
maltooligosaccharide + alpha,alpha'-trehalose
-
alpha-1,4-glucosidic and alpha-1,1-linked terminal dissaccharides of maltooligosyltrehalose
trehalose
-
?
maltosyltrehalose + H2O
maltose + alpha,alpha'-trehalose
-
-
-
?
maltohexaose + H2O
?
for glucose formation, maltohexaose exhibits the highest formation rate
-
-
?
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
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
-
?
maltotetraosyltrehalose + H2O
maltotetraose + alpha,alpha'-trehalose
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
-
?
maltotriosyltrehalose + H2O
maltotriose + alpha,alpha'-trehalose
-
-
-
?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
hydrolysis of G3T-G5T and G5-G7. Production of trehalose from starch together with isoamylase and maltooligosyltrehalose synthase, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Na+, K+, Mg2+, Ca2+, and Zn2+ do not activate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
EDTA, Na+, K+, Mg2+, Ca2+, and Zn2+ do not inhibit
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
EDTA does not activate. Expression levels of both wild-type and His-tagged MTHases are higher in the absence of IPTG than in the presence of 0.5 mM IPTG induction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
5.03
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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme H195A
1.14
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155A
5.54
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155F
28.2
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme R447A
47.3
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme D156A
144
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme E450A
182
maltooligosyltrehalose
-
pH 5, 60°C, calculated as the amount of trehalose released from the substrate, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
0.74
1.23
472
492
5.31
52
597
787
814
0.1
-
D380A MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
0.74
-
E286A MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
1.23
-
D255A MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
472
-
R356K MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
492
-
Y328F MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
5.31
-
W218A MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
52
-
W218F MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
597
-
F355Y MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
787
-
A259S MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
814
-
wild-type MTHase, hydrolysis of maltotetraosyltrehalose at 60°C in 50 mM citrate phosphate buffer, pH 5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5
-
wild-type, W218A, W218F, A259S, Y328F, F355Y, and R356K MTHases
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
60
85
85
-
wild-type, W218A, W218F, A259S, Y328F, F355Y, and R356K MTHases
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
129000
-
mass of wild-type and mutant enzymes, BioSep-SEC-S4000 gel filtration column
64000
2 * 64000, SDS-PAGE, 2 * 64240, electrospray ionization mass spectrometry, wild-type enzyme
64240
2 * 64000, SDS-PAGE, 2 * 64240, electrospray ionization mass spectrometry, wild-type enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
covalently linked by an intermolecular disulfide bond at residue C298
homodimer
2 * 64000, SDS-PAGE, 2 * 64240, electrospray ionization mass spectrometry, wild-type enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 4°C. The crystal structure of the E283Q mutant enzyme in complex with the substrate, maltotriosyltrehalose is determined to 2.6 A resolution. The structure with maltotriosyltrehalose indicates that the enzyme has at least five substrate binding subsites and that Glu283 is the catalytic acid, and Asp252 is the nucleophile that attacks the C1 carbon in the glycosidic linkage of maltotriosyltrehalose
hanging-drop vapor diffusion method, space group determined by precession photography: P3(2)21 or P3(1)21, cell dimensions: a = b = 80.2 A and c 0 281.9 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
A259S
D156A
-
kcat/Km for maltooligosyltrehalose is 3.8fold lower than wild-type value
D255A
D380A
E286A
E450A
-
kcat/Km for maltooligosyltrehalose is 1.2fold lower than wild-type value
F355Y
H195A
-
kcat/Km for maltooligosyltrehalose is 357fold lower than wild-type value
R356K
R447A
-
kcat/Km for maltooligosyltrehalose is 6.5fold lower than wild-type value
W218A
W218F
Y155A
-
kcat/Km for maltooligosyltrehalose is 160fold lower than wild-type value
Y155F
-
kcat/Km for maltooligosyltrehalose is 33fold lower than wild-type value
Y328F
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
all enzyme activity retained after 2 hours at 80°C, wild-type, W218A, W218F, A259S, Y328F, F355Y, and R356K MTHases
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli by anion exchange chromatography and gel filtration
wild-type enzyme purified by heat treatment, nucleic acid precipitation, and ion-exchange chromatography, 12fold. His-tagged MTHase partially purified from the cell-free extract directly by metal chelating chromatography, 14.7fold
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene treZ, recombinant enzyme expression in Brevibacillus brevis from pET-24a(+)-treZ-fused to pSVN resulting in 170 /g wet cell
Escherichia coli Rosetta (DE3) with mutated vector pET-15b-deltaH-treZ, Terrific broth, 37°C
-
expression of wild-type and mutant enzymes in Escherichia coli
pET-15b-deltaH-treZ vector expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
trehalose is gaining applications as sweetener component, preservative or stabilizer of food, cosmetics, vaccines, medicines, cells, and organs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Feese, M.D.; Kato, Y.; Tamada, T.; Kato, M.; Komeda, T.; Miura, Y.; Hirose, M.; Hondo, K.; Kobayashi, K.; Kuroki, R.
Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus
J. Mol. Biol.
301
451-464
2000
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus, Saccharolobus solfataricus KM1 (Q55088)
Fang, T.Y.; Tseng, W.C.; Guo, M.S.; Shih, T.Y.; Hung, X.G.
Expression, purification, and characterization of the maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
J. Agric. Food Chem.
54
7105-7112
2006
Saccharolobus solfataricus (P95867)
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
J. Agric. Food Chem.
56
562-533
2008
Saccharolobus solfataricus (P95867), Saccharolobus solfataricus P2 (P95867)
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
J. Agric. Food Chem.
56
5628-5633
2008
Saccharolobus solfataricus
Kato, M.; Miura, Y.; Kettoku, M.; Komeda, T.; Iwamatsu, A.; Kobayashi, K.
Reaction mechanism of a new glycosyltrehalose-hydrolyzing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1
Biosci. Biotechnol. Biochem.
60
925-928
1996
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus KM1 (Q55088)
Kato, M.
Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1
J. Mol. Catal. B
6
223-233
1999
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus KM1 (Q55088)
-
Kobayashi, K.; Kato, M.; Miura, Y.; Kettoku, M.; Komeda, T.; Iwamatsu, A.
Gene cloning and expression of new trehalose-producing enzymes from the hyperthermophilic archaeum Sulfolobus solfataricus KM1
Biosci. Biotechnol. Biochem.
60
1882-1885
1996
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus KM1 (Q55088)
Fu, C.W.; Wang, Y.P.; Fang, T.Y.; Lin, T.H.
Interaction between trehalose and MTHase from Sulfolobus solfataricus studied by theoretical computation and site-directed mutagenesis
PLoS One
8
e68565
2013
Saccharolobus solfataricus, Saccharolobus solfataricus KM1
Okazaki, N.; Tamada, T.; Feese, M.D.; Kato, M.; Miura, Y.; Komeda, T.; Kobayashi, K.; Kondo, K.; Blaber, M.; Kuroki, R.
Substrate recognition mechanism of a glycosyltrehalose trehalohydrolase from Sulfolobus solfataricus KM1
Protein Sci.
21
539-552
2012
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus KM1 (Q55088)
Wu, S.; Su, L.; Yao, K.; Wu, J.; Wu, D.
Heterologous expression of MTSase and MTHase in Brevibacillus brevis and its application
J. Food Sci. Biotechnol.
37
838-844
2018
Saccharolobus solfataricus (Q55088), Saccharolobus solfataricus ATCC 33909 (Q55088)
-
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