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Information on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase and Organism(s) Thermus thermophilus and UniProt Accession O06458
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5.4.99.16 maltose alpha-D-glucosyltransferaseSpecify your search results
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- 5.4.99.16
- methyltransferase
- endonuclease
- cap
-
restriction-modification
- s-adenosyl-l-methionine
- adomet
- s-adenosylmethionine
-
nonstructural
-
enase
- sinefungin
- flavivirus
- trehalose-6-phosphate
-
adomet-dependent
- hpaii
- dengue
- coronaviruses
-
sam-binding
- medicine
- smrt
-
adohcy
- nsp1
-
adomet-binding
- o6-methylguanine
- n6-methyladenine
-
cytosine-5-methyltransferase
-
guanylyltransferase
-
n6-adenine
-
isoschizomer
- trehalase
-
photoelectrochemical
- synthesis
-
cytosine-5
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mtase, trehalose synthase, tttres, trehalose synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
57-KDa trehalose synthase (Saccharomyces cerevisiae)
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Maltose alpha-D-glucosylmutase
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Maltose alpha-D-glucosyltransferase
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Maltose glucosylmutase
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Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced)
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Protein (Saccharomyces cerevisiae gene CIF1 reduced)
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Synthase, trehalose
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Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
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Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
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Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
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Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
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Trehalose synthase
Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
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Trehalose synthetase
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TreS
Trehalose synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
maltose = alpha,alpha-trehalose
two-step, double displacement mechanism of the enzyme, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl bond isomerization
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SYSTEMATIC NAME
IUBMB Comments
maltose alpha-D-glucosylmutase
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CAS REGISTRY NUMBER
COMMENTARY
147994-22-7
protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced) /57-KDa trehalose synthase (Saccharomyces cerevisiae gene CIF1) /protein (Saccharomyces cerevisiae gene CIF1 reduced) /synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
178604-93-8
synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced) /trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
187285-67-2
synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
211621-92-0
synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
395644-91-4
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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
maltose
alpha,alpha-trehalose + D-glucose + maltose
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the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
starch
alpha,alpha-trehalose
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substrate of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
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-
?
additional information
?
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the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
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-
?
additional information
?
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the enzyme yields 80% trehalose from 800 mM maltose at 30°C in 48 h
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-
?
additional information
?
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the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
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-
?
additional information
?
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the enzyme yields 74% trehalose from 292 mM maltose at 50°C in 10 h
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-
?
additional information
?
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the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
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-
?
additional information
?
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the wild-type enzyme retains the glucose moiety in the active site during the reaction to effectively produce trehalose. 13C NMR analysis is performed to identify the glycosidic structure of the purified transfer disaccharide product, where the carbon signals are compared with that of alpha-mannose. Activity analysis by thin-layer chromatography
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-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Hg2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Pb2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Tris
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Zn2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
62
alpha,alpha-trehalose
recombinant His6-tagged wild-type enzyme, pH 6.5, 50°C
69.6
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant mutant TSMrTt
82.2
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant wild-type enzyme
154
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant mutant TSTtMr
456
alpha,alpha-trehalose
recombinant His6-tagged mutant DM2, pH 6.5, 50°C
1551
alpha,alpha-trehalose
recombinant His6-tagged mutant DM1, pH 6.5, 50°C
48
maltose
recombinant His6-tagged wild-type enzyme, pH 6.5, 50°C
additional information
additional information
Michaelis-Menten kinetics of recombinant His6-tagged wild-type and mutant enzymes
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additional information
additional information
-
Michaelis-Menten kinetics of recombinant His6-tagged wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.871
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant mutant TSMrTt
1.32
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant mutant TSTtMr
1.33
alpha,alpha-trehalose
pH 6.5, 30°C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
pH optimum for enzyme and for recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
6.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
both deletion mutant lacking 415 amino acids from C-terminus, and fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus
50
70
-
temperature optimum for enzyme and for recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the C-terminal domain of the three-domain-comprising trehalose synthase from Thermus thermophilus is truncated in order to study the effect on the enzyme's activity and substrate specificity. Two truncated enzymes (DM1 and DM2) show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose. Mutant DM1 synthesizes much higher amounts of mannose-containing disaccharide trehalose analogue (Man-TA) than does the wild-type or mutant DM2. The mutant enzymes could be used to produce Man-TA, a postulatedinhibitor of gut disaccharidases
additional information
additional information
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the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the C-terminal domain in the wild-type enzyme is important for retaining the glucose moiety of the substrate within the active site
additional information
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the C-terminal domain in the wild-type enzyme is important for retaining the glucose moiety of the substrate within the active site
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
164000
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
61000
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
106000
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
106000
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
?
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
additional information
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure analysis and modeling, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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use of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa for production of trehalose from starch. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
additional information
additional information
the C-domain of enzyme TtTreS, TtTreS-C, is fused to four different enzymes from other species, i.e. PpTreS, CgTreS, ScTreS, and TmTreS from Pseudomonas putida NBRC 14164, Corynebacterium glutamicum ATCC 13032, Streptomyces coelicolor ATCC 23899, and Thermotoga maritima MSB8, domain structures, overview. A flexible linker peptide between the TreS enzyme and TtTreS-C is essential for its activity enhancement. The specific activities of the four enzymes are improved by linking to the TtTreS-C fragment. When added with the C-terminal domain of TtTreS, the thermostability of a cold-active TreS from Deinococcus radiodurans (DrTreS) is greatly improved
additional information
-
the C-domain of enzyme TtTreS, TtTreS-C, is fused to four different enzymes from other species, i.e. PpTreS, CgTreS, ScTreS, and TmTreS from Pseudomonas putida NBRC 14164, Corynebacterium glutamicum ATCC 13032, Streptomyces coelicolor ATCC 23899, and Thermotoga maritima MSB8, domain structures, overview. A flexible linker peptide between the TreS enzyme and TtTreS-C is essential for its activity enhancement. The specific activities of the four enzymes are improved by linking to the TtTreS-C fragment. When added with the C-terminal domain of TtTreS, the thermostability of a cold-active TreS from Deinococcus radiodurans (DrTreS) is greatly improved
additional information
the crude TtTreS is immobilized on the surface of glutaraldehyde-3-aminopropyltriethoxysilane-silicalite-1 (GA-APS-silicalite-1, silicalite-1 modified sequentially with 3-aminopropyltriethoxysilane and glutaraldehyde) without enzyme purification. In this case, a nucleophilic attack takes place at the aldehyde group of glutaraldehyde by the amino group of the protein to form a Schiff base. Preparation of activated silicalite-1, APS-silicalite-1, and GA-APS-silicalite-1 and enzyme immobilization, method optimization, overview. Immobilization also provides TtTreS with potential application in a relatively wide range of temperatures from 40°C to 70°C. The trehalose yield of immobilized TtTreS in first cycle reaches 61.52%. After 22 cycles of enzymatic reaction, the immobilized TtTreS still retains 81% of its initial trehalose yield
additional information
deletion mutant lacking 415 amino acids from C-terminus has a lower thermostability and produces more byproducts than wild-type. Fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
-
deletion mutant lacking 415 amino acids from C-terminus has a lower thermostability and produces more byproducts than wild-type. Fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
-
construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
construction of two truncated enzymes (DM1 and DM2), which show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose
additional information
-
construction of two truncated enzymes (DM1 and DM2), which show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose
additional information
-
enzyme expression in Escherichia coli strain Rosetta (DE3) for trehalose production, method optimization to 50°C, pH 9.0, 10 h, 10% maltose solution, and co-expression of molecular chaperones sigma32, GroEL, GroES, DnaK and DnaJ greatly increasing the solubility of the trehalose synthase protein. Addition of Ca2+ and DTT increase the activity by 19% and 41%, respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
both enzyme and recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa, stable
680294
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
half-lives of purified wild-type enzyme: over 480 min, purified mutant TSMrTt : 47.6 min, and purified mutant TSTtMr: over 480 min
70 - 80
-
the half-life of heat inactivation for free and chitosan-immobilized enzymes is 5.7 and 6.3 days at 70°C, respectively. The free enzyme displays complete loss of activity after 8 days at 80°C, whereas the chitosan-immobilized enzyme still retains about 25% of the initial activity
75
half-lives of purified wild-type enzyme: 475 min, purified mutant TSMrTt : 17.6 min, and purified mutant TSTtMr: over 480 min
80
additional information
80
30 min, wild-type, 88% residual activity, fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, 83% residual activity
80
half-lives of purified wild-type enzyme: 233 min, purified mutant TSMrTt : below 5 min, and purified mutant TSTtMr: 27.6 min
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
-
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
when tested in batch reaction, the immobilized enzyme retains its relative activity of 53% after 30 reuses of reaction within 12 days
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme and domainC-fusion mutant enzymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration
recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase and vice versa having both activities
-
recombinant His6-tagged wild-type and chimeric mutant enzymes from Escherichia coli strain Rosetta-gami (DE3) by nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene treS, sequence comparisons, recombinant expression of His-tagged wild-type enzyme and mutant enzymes from other species that are fused to the domain C from the Thermus thermophilus enzyme, in Escherichia coli strain Rosetta (DE3)
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
construction of fusion genes from beta-amylase gene of Clostridium thermofluorogenes and trehalose synthase and overexpression in Escherichia coli
-
gene treS, sequence comparison, expression of His6-tagged wild-type enzyme and chimeric mutant in Escherichia coli strain Rosetta-gami (DE3), subcloning in Escherichia coli strain DH5alpha
recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3). Plasmids with different promoters and copy numbers are important for the expression of trehalose synthase genes in Escherichia coli. The trehalose synthase from Thermus thermophilus is best expressed from plasmid pET-22b showing high activity in trehalose production with 1.996 U/mg protein, co-expression of molecular chaperones sigma32, GroEL, GroES, DnaK and DnaJ greatly increasing the solubility of the trehalose synthase protein
-
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
-
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, J.H.; Tsai, M.Y.; Lee, G.C.; Shaw, J.F.
Construction of a recombinant thermostable beta-amylase-trehalose synthase bifunctional enzyme for facilitating the conversion of starch to trehalose
J. Agric. Food Chem.
55
1256-1263
2007
Thermus thermophilus
Wang, J.H.; Tsai, M.Y.; Chen, J.J.; Lee, G.C.; Shaw, J.F.
Role of the C-terminal domain of Thermus thermophilus trehalose synthase in the thermophilicity, thermostability, and efficient production of trehalose
J. Agric. Food Chem.
55
3435-3443
2007
Deinococcus radiodurans, Thermus thermophilus (Q7WUI5), Thermus thermophilus
Kim, H.J.; Kim, A.R.; Jeon, S.J.
Immobilization on chitosan of a thermophilic trehalose synthase from Thermus thermophilus HJ6
J. Microbiol. Biotechnol.
20
513-517
2010
Thermus thermophilus, Thermus thermophilus HJ6
Wang, Y.; Zhang, J.; Wang, W.; Liu, Y.; Xing, L.; Li, M.
Effects of the N-terminal and C-terminal domains of Meiothermus ruber CBS-01 trehalose synthase on thermostability and activity
Extremophiles
16
377-385
2012
Meiothermus ruber (B1PK99), Meiothermus ruber, Thermus thermophilus (Q5SL15), Thermus thermophilus, Meiothermus ruber CBS-01 (B1PK99), Meiothermus ruber CBS-01, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SL15)
Cai, X.; Seitl, I.; Mu, W.; Zhang, T.; Stressler, T.; Fischer, L.; Jiang, B.
Biotechnical production of trehalose through the trehalose synthase pathway current status and future prospects
Appl. Microbiol. Biotechnol.
102
2965-2976
2018
Corynebacterium glutamicum (A0A1R4FYB1), Corynebacterium glutamicum ATCC 13032 (A0A1R4FYB1), Deinococcus geothermalis (Q1J0Z5), Deinococcus geothermalis DSMZ 11300 (Q1J0Z5), Deinococcus radiodurans (I3NX86), Deinococcus radiodurans (Q9RST7), Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 (I3NX86), Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 (Q9RST7), Enterobacter hormaechei (F5S1H2), Enterobacter hormaechei ATCC 49162 (F5S1H2), Meiothermus ruber (B1PK99), Mycobacterium tuberculosis (P9WQ19), Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WQ19), Mycolicibacterium smegmatis (A0R6E0), Mycolicibacterium smegmatis ATCC 700084 / mc2_155 (A0R6E0), Paenarthrobacter aurescens (B8YM30), Picrophilus torridus (Q6L2Z7), Picrophilus torridus DSM 9790 (Q6L2Z7), Pseudomonas sp. P8005 (I3WCP4), Pseudomonas stutzeri (A0A4S2BJW1), Pseudomonas stutzeri CJ38 (A0A4S2BJW1), Rhodococcus opacus (M1PA89), Rhodococcus opacus ATCC 41021 (M1PA89), Thermobaculum terrenum (D1CE96), Thermobifida fusca (Q47SE5), Thermobifida fusca DSM 43792 (Q47SE5), Thermomonospora curvata (D1ABU6), Thermomonospora curvata DSM 43183 (D1ABU6), Thermus thermophilus, Thermus thermophilus (O06458), Thermus thermophilus ATCC 33923 (O06458)
Li, Y.; Wang, Z.; Feng, Y.; Yuan, Q.
Improving trehalose synthase activity by adding the C-terminal domain of trehalose synthase from Thermus thermophilus
Biores. Technol.
245
1749-1756
2017
Streptomyces coelicolor, Thermotoga maritima, Corynebacterium glutamicum (A0A1R4FYB1), Pseudomonas putida (A0A2Z4RCL2), Deinococcus radiodurans (I3NX86), Thermus thermophilus (O06458), Thermus thermophilus, Corynebacterium glutamicum ATCC 13032 (A0A1R4FYB1), Streptomyces coelicolor ATCC 23899, Pseudomonas putida NBRC 14164 (A0A2Z4RCL2), Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 (I3NX86)
Li, Y.; Sun, X.; Feng, Y.; Yuan, Q.
Cloning, expression and activity optimization of trehalose synthase from Thermus thermophilus HB27
Chem. Eng. Sci.
135
323-329
2017
Thermus thermophilus
-
Cho, C.B.; Park, D.Y.; Lee, S.B.
Effect of C-terminal domain truncation of Thermus thermophilus trehalose synthase on its substrate specificity
Enzyme Microb. Technol.
96
121-126
2017
Thermus thermophilus (Q7WUI5), Thermus thermophilus, Thermus thermophilus ATCC 33923 (Q7WUI5)
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