Information on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
5.4.99.16
-
RECOMMENDED NAME
GeneOntology No.
maltose alpha-D-glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
maltose = alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose = alpha,alpha-trehalose
show the reaction diagram
two-step, double displacement catalytic mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl bond isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
-
trehalose biosynthesis IV
-
-
SYSTEMATIC NAME
IUBMB Comments
maltose alpha-D-glucosylmutase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57-KDa trehalose synthase (Saccharomyces cerevisiae)
-
-
-
-
Maltose alpha-D-glucosylmutase
-
-
-
-
Maltose alpha-D-glucosyltransferase
-
-
-
-
Maltose glucosylmutase
-
-
-
-
Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced)
-
-
-
-
Protein (Saccharomyces cerevisiae gene CIF1 reduced)
-
-
-
-
Synthase, trehalose
-
-
-
-
Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
-
-
-
-
Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
-
-
-
-
Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
-
-
-
-
Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
-
-
-
-
Trehalose synthase
-
-
-
-
Trehalose synthase
A8QX00
-
Trehalose synthase
A8QX00
-
-
Trehalose synthase
B8YM30
-
Trehalose synthase
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
-
Trehalose synthase
-
-
Trehalose synthase
Corynebacterium glutamicum ATCC13032
-
-
-
Trehalose synthase
Q9RST7
-
Trehalose synthase
Deinococcus radiodurans DSMZ 20539
Q9RST7
-
-
Trehalose synthase
B6E9W1
-
Trehalose synthase
-
-
Trehalose synthase
B1PK99
-
Trehalose synthase
Meiothermus ruber CBS-01
B1PK99
-
-
Trehalose synthase
-
-
Trehalose synthase
A0R6E0
-
Trehalose synthase
Mycobacterium smegmatis ATCC 700084
A0R6E0
-
-
Trehalose synthase
-
-
Trehalose synthase
-
-
Trehalose synthase
Pseudomonas putida P06
-
-
-
Trehalose synthase
-
-
Trehalose synthase
-
-
Trehalose synthase
Q5SL15
-
Trehalose synthase
Thermus thermophilus HJ6
-
-
-
Trehalose synthase
-
-
Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
-
-
-
-
Trehalose synthetase
-
-
-
-
TreS
A8QX00
-
TreS
A8QX00
-
-
TreS
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
-
TreS
Corynebacterium glutamicum ATCC13032
-
-
-
TreS
Deinococcus radiodurans DSMZ 20539
Q9RST7
-
-
TreS
B1PK99
-
TreS
Meiothermus ruber CBS-01
B1PK99
-
-
TreS
Mycobacterium smegmatis ATCC 700084
A0R6E0
-
-
TreS
Pseudomonas putida P06
-
-
-
TSase
Thermus thermophilus HJ6
-
-
-
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
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain CGMCC 1.1892
UniProt
Manually annotated by BRENDA team
Arthrobacter aurescens CGMCC 1.1892
strain CGMCC 1.1892
UniProt
Manually annotated by BRENDA team
Corynebacterium glutamicum ATCC13032
-
-
-
Manually annotated by BRENDA team
locus Dgeo-0537
UniProt
Manually annotated by BRENDA team
Deinococcus geothermalis 11300
locus Dgeo-0537
UniProt
Manually annotated by BRENDA team
locus DR-2036
UniProt
Manually annotated by BRENDA team
Deinococcus radiodurans DSMZ 20539
locus DR-2036
UniProt
Manually annotated by BRENDA team
gene treS
Uniprot
Manually annotated by BRENDA team
strain CBS-01
Uniprot
Manually annotated by BRENDA team
Meiothermus ruber CBS-01
gene treS
Uniprot
Manually annotated by BRENDA team
Mycobacterium smegmatis ATCC 700084
-
UniProt
Manually annotated by BRENDA team
strain R48
-
-
Manually annotated by BRENDA team
Pimelobacter sp. R48
strain R48
-
-
Manually annotated by BRENDA team
gene treS
-
-
Manually annotated by BRENDA team
Pseudomonas putida P06
gene treS
-
-
Manually annotated by BRENDA team
strain F1
-
-
Manually annotated by BRENDA team
strain F1
-
-
Manually annotated by BRENDA team
ATCC 33923
-
-
Manually annotated by BRENDA team
gene treS
UniProt
Manually annotated by BRENDA team
strain HJ6
-
-
Manually annotated by BRENDA team
Thermus thermophilus HJ6
strain HJ6
-
-
Manually annotated by BRENDA team
isolated from saline-alkali soil, gene treS
-
-
Manually annotated by BRENDA team
Meiothermus ruber CBS-01
strain CBS-01
Uniprot
Manually annotated by BRENDA team
additional information
no activity in Thermoproteus tenax strain Kra1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
A0R6E0
the enzyme belongs to glycoside hydrolase family GH13
evolution
-
the enzyme belongs to the glycosyl hydrolase family 13
evolution
-
the enzyme is a retaining alpha-transglycosidase in the alpha-amylase family (GH13)
evolution
Mycobacterium smegmatis ATCC 700084
-
the enzyme belongs to glycoside hydrolase family GH13
-
metabolism
A0R6E0
trehalose synthase catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide
physiological function
A0R6E0
importance of trehalose to survival of mycobacteria, possible association of the enzyme with glycogen enhances its role in glycogen biosynthesis and degradation
physiological function
-
the enzyme functions primarily in the mobilization of trehalose as a glycogen precursor
physiological function
Mycobacterium smegmatis ATCC 700084
-
importance of trehalose to survival of mycobacteria, possible association of the enzyme with glycogen enhances its role in glycogen biosynthesis and degradation
-
metabolism
Mycobacterium smegmatis ATCC 700084
-
trehalose synthase catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide
-
additional information
A0R6E0
determination and analysis of the structure of the enzyme and of the enzyme in complex with acarbose, oligosaccharide-binding site within the C-terminal domain, catalytic site structure, overview. Structure-function analysis
additional information
B1PK99
enzyme structure analysis and molecular modeling, overview
additional information
-
the highly conserved Asp294 residue is critical for catalytic activity, homology modeling and flexible docking studies of the enzyme-substrate system, overview
additional information
Meiothermus ruber CBS-01
-
enzyme structure analysis and molecular modeling, overview
-
additional information
Mycobacterium smegmatis ATCC 700084
-
determination and analysis of the structure of the enzyme and of the enzyme in complex with acarbose, oligosaccharide-binding site within the C-terminal domain, catalytic site structure, overview. Structure-function analysis
-
additional information
Pseudomonas putida P06
-
the highly conserved Asp294 residue is critical for catalytic activity, homology modeling and flexible docking studies of the enzyme-substrate system, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose
maltose
show the reaction diagram
B1PK99
-
-
-
r
alpha,alpha-trehalose
maltose
show the reaction diagram
Q5SL15
-
-
-
?
alpha,alpha-trehalose
maltose
show the reaction diagram
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose
-
-
r
alpha,alpha-trehalose
maltose
show the reaction diagram
Meiothermus ruber CBS-01
B1PK99
-
-
-
r
high-maltose rice syrup
alpha,alpha-trehalose
show the reaction diagram
-
-
the highest alpha,alpha-trehalose yield (54.6%) can be obtained by 3.5 units/maltose (g) of trehalose synthase from the maltose syrup at 50C for 20-24 h
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
A8QX00
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
B6E9W1
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
B1PK99
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Q1J0Z5
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q9RST7
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q5SL15
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
A0R6E0
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
30% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q7WUI5
-
wild-type, 80% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
wild-type, 92% yield
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
B8YM30
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
r
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
-
ratio of kcat to Km value is 2.5fold higher for maltose than for trehalose. Maximum conversion rate for maltose into trehalose is independent of substrate concentration and reaches 71% at 20C
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
B1PK99
the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate
TreS also has a weak hydrolytic property with D-glucose as the byproduct
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
the maximum conversion yield reaches 69% at 25C after 9 h of reaction
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
one-step conversion via intramolecular transglucosylation reaction
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
the recombinant enzyme has a 4.1fold higher catalytic efficientcy for maltose than for trehalose
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
A0R6E0
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Deinococcus geothermalis 11300
Q1J0Z5
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Meiothermus ruber CBS-01
B1PK99
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Pimelobacter sp. R48
-
r
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
A8QX00
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Mycobacterium smegmatis ATCC 700084
A0R6E0
two-step, double-displacement mechanism
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Deinococcus radiodurans DSMZ 20539
Q9RST7
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
maltose
alpha,alpha-trehalose
show the reaction diagram
Pseudomonas putida P06
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Arthrobacter aurescens CGMCC 1.1892
B8YM30
-
as a byproduct, about 13% glucose is also produced
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Corynebacterium glutamicum ATCC13032
-
the maximum conversion yield reaches 69% at 25C after 9 h of reaction
-
-
r
starch
?
show the reaction diagram
-
-
-
-
?
starch
alpha,alpha-trehalose
show the reaction diagram
-
substrate of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa. Catalytic efficiency of fusion protein is higher than that of a mixture of individual enzymes
-
-
?
Sucrose
Trehalulose
show the reaction diagram
-
activity is very low compared to that with maltose
i.e. 1-O-alpha-D-glucopyranosyl-D-fructose
-
sucrose
D-glucose + D-fructose + [alpha-D-glucopyranosyl-(1,1)-D-fructofuranose]
show the reaction diagram
-
low activity on sucrose
-
-
?
maltose
alpha,alpha-trehalose + D-glucose + maltose
show the reaction diagram
Thermus thermophilus, Thermus thermophilus HJ6
-
-
the product is composed of alpha,alpha-trehalose (48%), D-glucose (20%), maltose (32%)
-
?
additional information
?
-
-
no substrates: glucose, fructose, lactose, sucrose, starch
-
-
-
additional information
?
-
A8QX00
does not use acarbose and glucose as substrates
-
-
-
additional information
?
-
-
TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
-
-
-
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of alpha-aryl glucosides as well as alpha-glucosyl fluoride, overview. Reaction of TreS with 5-fluoro-alpha-D-glucosyl fluoride results in the trapping of a covalent glycosyl-enzyme intermediate consistent with TreS being a member of the retaining glycoside hydrolase family 13 enzyme family, thus likely following a two-step, double displacement mechanism. Inability of TreS to incorporate isotope-labeled exogenous glucose into maltose or trehalose, the absence of a secondary deuterium kinetic isotope effect and the general independence of kcat upon leaving group ability both point to a rate-determining conformational change, likely the opening and closing of the enzyme active site
-
-
-
additional information
?
-
A0R6E0
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
-
additional information
?
-
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
-
additional information
?
-
A8QX00
does not use acarbose and glucose as substrates
-
-
-
additional information
?
-
Mycobacterium smegmatis ATCC 700084
A0R6E0
trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity
-
-
-
additional information
?
-
Pseudomonas putida P06
-
TreS interconverts maltose and trehalose by an intramolecular mechanism, and therefore does not require external glucose or any other factors during the enzymatic reaction
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
B1PK99
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Q9RST7
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Q5SL15
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
A0R6E0
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
-
one-step conversion via intramolecular transglucosylation reaction
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Meiothermus ruber CBS-01
B1PK99
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Mycobacterium smegmatis ATCC 700084
A0R6E0
-
-
-
r
maltose
alpha,alpha-trehalose
show the reaction diagram
Deinococcus radiodurans DSMZ 20539
Q9RST7
-
-
-
?
maltose
alpha,alpha-trehalose
show the reaction diagram
Pseudomonas putida P06
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
B8YM30
123% relative activity at 1 mM
Ca2+
A0R6E0
hepta-coordinated calcium-ion-binding site located about 13 A from the active site at the interface between domain A and domain B, enzyme binding structure, overview
Cl-
A0R6E0
enzyme binding structure of 4 Cl- ions, overview
Fe2+
-
114% activity at 1 mM
K+
-
10 mM, 22% increase in activity
Mg2+
-
10 mM, 29% increase in activity
Mg2+
B8YM30
118% relative activity at 1 mM
Mg2+
-
112% activity at 1 mM
Mg2+
A0R6E0
hexa-coordinated magnesium ion located in the solvent-accessible loop L1, residues 50-60, of domain A, about 25 A from the catalytic center, enzyme binding structure, overview. Interactions with this magnesium ion come from Asp51, Asn53, Asp55, Ile57, Asp59 and one water molecule
Mn2+
B8YM30
116% relative activity at 1 mM
Mn2+
B6E9W1
Mn2+ shows an enhancing effect by 11% at 1 mM
additional information
B6E9W1
TreS activity is not affected by NH4+, Ca2+, and Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-fluoro-alpha-D-glucosyl fluoride
-
behaves like a reversible inhibitor
-
acarbose
A0R6E0
competitively inhibited by the potent alpha-glucosidase inhibitor acarbose, acarbose-binding site structure, overview
Al3+
-
1 mM, complete inhibition
Al3+
B1PK99
complete inhibition at 2 mM
Al3+
Q9RST7
98.5% inhibition at 1 mM
Al3+
-
complete inhibition at 2 mM, 8% inhibition of aggregated enzyme
beta-mercaptoethanol
B6E9W1
complete inhibition at 1 mM
Ca2+
-
the MTase activity of TreS is inhibited by 5 mM Ca2+ and other divalent cations
Ca2+
B8YM30
98% residual activity at 5 mM
Ca2+
B1PK99
about 10% residual activity at 10 mM
Ca2+
-
93% residual activity at 5 mM
Ca2+
Q9RST7
13.4% inhibition at 10 mM, 9.5% at 1 mM
Cd2+
-
slight inhibition
Co2+
B1PK99
about 5% residual activity at 10 mM
Co2+
Q1J0Z5
1 mM, 55% residual activity
Co2+
Q9RST7
17.2% inhibition at 1 mM
Cu2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Cu2+
-
10 mM, 85% residual activity
Cu2+
B8YM30
complete inhibition at 5 mM
Cu2+
B1PK99
complete inhibition at 2 mM
Cu2+
B6E9W1
52% residual activity at 1 mM
Cu2+
-
45.4% residual activity at 5 mM
Cu2+
Q1J0Z5
1 mM, 5% residual activity
Cu2+
Q9RST7
complete inhibition at 10 mM
Cu2+
-
complete inhibition at 2 mM, 23% inhibition of aggregated enzyme
D-gluconohydroximino-1,5-lactam
-
-
-
D-glucose
B1PK99
in the presence of 10 mM D-glucose, TreS shows a 3.6fold increase in Km and a nearly unchanged Vmax for maltose, implying that D-glucose is a competitive inhibitor of TreS
deoxynojirimycin
-
-
dithiotreitol
Q9RST7
9% inhibition at 5 mM, 12% at 10 mM
-
EDTA
B8YM30
86% residual activity at 5 mM
EDTA
-
68.5% residual activity at 5 mM
EDTA
Q1J0Z5
inhibitory above 1 mM
EDTA
Q9RST7
15% inhibition at 1 mM, 35% at 10 mM
Fe2+
B1PK99
complete inhibition at 2 mM
Fe2+
B6E9W1
92% residual activity at 1 mM
Fe2+
-
95% inhibition at 2 mM, 5% inhibition of aggregated enzyme
Fe3+
Q1J0Z5
1 mM, 60% residual activity
Guanidine-HCl
-
complete inhibition at 1 M, 51% inhibition of aggregated enzyme
Hg2+
-
1 mM, complete inhibition
Hg2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Hg2+
B6E9W1
57% residual activity at 1 mM
Hg2+
Q1J0Z5
1 mM, 15% residual activity
Hg2+
Q9RST7
complete inhibition at 1 mM
Mg2+
B8YM30
92% residual activity at 5 mM
Mg2+
Q1J0Z5
1 mM, 75% residual activity
Mg2+
Q9RST7
8.5% inhibition at 1-10 mM
Mn2+
-
10 mM, 60% residual activity
Mn2+
B8YM30
86% residual activity at 5 mM
Mn2+
B1PK99
about 10% residual activity at 10 mM
Mn2+
-
60.9% residual activity at 5 mM
Na+
B6E9W1
90% residual activity at 1 mM
Ni2+
B1PK99
about 10% residual activity at 10 mM
Ni2+
-
49.4% residual activity at 5 mM
Ni2+
Q9RST7
28.5% inhibition at 1mM, 45% at 10 mM
Pb2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Pb2+
-
slight inhibition
SDS
B8YM30
complete inhibition at 1 mM
SDS
B6E9W1
10% residual activity at 1 mM
SDS
-
0.25% residual activity at 5 mM
SDS
Q9RST7
95.1% inhibition at 5 mM
sodium dodecylsulfate
-
1 mM, complete inhibition
Sucrose
-
competitive inhibition of the interconversion between maltose and trehalose
Tris
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Tris
Q1J0Z5
10 mM, 9% residual activity
Tris
Q9RST7
58% inhibition at 5 mM, 78% at 10 mM
Tris
-
complete inhibition at 25 mM, 23% inhibition of aggregated enzyme
Urea
-
90% inhibition at 2 M, 1% inhibition of aggregated enzyme
validoxylamine
-
strong inhibition
xylodeoxynojirimycin
-
-
-
Zn2+
-
inhibition of recombinant fusion protein with N-terminal beta-amylase of Clostridium thermofluorogenes and C-terminal trehalose synthase or vice versa
Zn2+
-
10 mM, 20% residual activity
Zn2+
B1PK99
complete inhibition at 2 mM
Zn2+
B6E9W1
59% residual activity at 1 mM
Zn2+
-
71.6% residual activity at 5 mM
Zn2+
Q1J0Z5
1 mM, 29% residual activity
Zn2+
Q9RST7
complete inhibition at 5 mM
Zn2+
-
92% inhibition at 2 mM, 1% inhibition of aggregated enzyme
Mn2+
Q9RST7
20% inhibition at 1 mM, 30% at 10 mM
additional information
-
not inhibited by acarbose
-
additional information
B6E9W1
TreS activity is not affected by EDTA
-
additional information
-
no or poor inhibition by MgCl2, MnCl, BaCl2, CaCl2, SrCl2, NiCl2, CoCl2Al2(SO4), FeSO4, DTT, and EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
Q1J0Z5
1 mM, 110% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.087
alpha,alpha-trehalose
-
pH 6.8, 37C
69.6
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
69.6
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant mutant TSMrTt
75
alpha,alpha-trehalose
B6E9W1
in 50 mM phosphate buffer (pH 6) at 37C
82.2
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant wild-type enzyme
90
alpha,alpha-trehalose
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
98.9
alpha,alpha-trehalose
B1PK99
-
98.9
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
154
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
154
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant mutant TSTtMr
0.008
maltose
-
pH 6.8, 37C
1.1
maltose
-
-
10
maltose
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
25
maltose
B6E9W1
in 50 mM phosphate buffer (pH 6) at 37C
34.5
maltose
-
-
42.4
maltose
-
45C, pH 6.0
57.5
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
57.5
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSTtMr
79.2
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
79.2
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSMrTt
97.4
maltose
Q5SL15
pH 6.5, 30C, recombinant wild-type enzyme
126
maltose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
126.2
maltose
B1PK99
-
137.8
maltose
-
45C, pH 6.0, presence of 10 mM glucose
254
maltose
Q1J0Z5
pH 7.6, 40C
96.5
Sucrose
-
-
26
trehalose
-
-
158
trehalose
-
-
210.3
trehalose
-
45C, pH 6.0
290.7
maltose
Q9RST7
pH 7.6, 30C, recombinant His6-tagged enzyme
additional information
additional information
-
Michaelis-Menten steady-state kinetics with 5-fluoroglycosyl fluorides, alpha-aryl glucosides, and alpha-glucosyl fluoride
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
61
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
66
alpha,alpha-trehalose
-
pH 6.8, 37C
68.9
alpha,alpha-trehalose
B1PK99
-
68.9
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
110
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
202
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
19
maltose
-
pH 6.8, 37C
31.9
maltose
Q1J0Z5
pH 7.6, 40C
95
maltose
-
45C, pH 6.0
97.8
maltose
-
45C, pH 6.0, presence of 10 mM glucose
115
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
115
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSMrTt
147
maltose
B1PK99
-
147
maltose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
152
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
152
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSTtMr
227
maltose
Q5SL15
pH 6.5, 30C, recombinant wild-type enzyme
187.6
trehalose
-
45C, pH 6.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.697
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
589
0.7
alpha,alpha-trehalose
B1PK99
-
589
0.75
alpha,alpha-trehalose
-
pH 6.8, 37C
589
0.871
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
589
0.871
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant mutant TSMrTt
589
1.32
alpha,alpha-trehalose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
589
1.32
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant mutant TSTtMr
589
1.33
alpha,alpha-trehalose
Q5SL15
pH 6.5, 30C, recombinant wild-type enzyme
589
1.16
maltose
B1PK99
pH 6.5, 30C, recombinant wild-type enzyme
86
1.17
maltose
B1PK99
-
86
1.5
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSMrTt
86
1.5
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSMrTt
86
2.4
maltose
-
pH 6.8, 37C
86
2.51
maltose
Q5SL15
pH 6.5, 30C, recombinant wild-type enzyme
86
2.7
maltose
B1PK99
pH 6.5, 30C, recombinant mutant TSTtMr
86
2.7
maltose
Q5SL15
pH 6.5, 30C, recombinant mutant TSTtMr
86
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
casuarine
-
pH 6.8, 37C
0.0021
D-gluconohydroximino-1,5-lactam
-
pH 6.8, 37C
-
3.76
D-glucose
B1PK99
-
0.00025
deoxynojirimycin
-
pH 6.8, 37C
0.14
isofagomine
-
pH 6.8, 37C
0.000025
validoxylamine
-
in 40 mM potassium phosphate buffer (pH 6.8), at 37C
0.3
xylodeoxynojirimycin
-
pH 6.8, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
-
cell-free extract, at pH 6.0 and 45C for 25 min using maltose as substrate
0.25
-
after 5.3fold purification, at pH 6.0 and 45C for 25 min using maltose as substrate
0.96
-
Mn2+-loaded, immobilized enzyme at pH 6.0 and 40C
1.17
-
Fe3+-loaded, immobilized enzyme at pH 6.0 and 40C
1.55
-
Cu2+-loaded, immobilized enzyme at pH 6.0 and 40C
2.84
-
Ni2+-loaded, immobilized enzyme at pH 6.0 and 40C
3.3
-
Zn2+-loaded, immobilized enzyme at pH 6.0 and 40C
3.98
-
Co2+-loaded, immobilized enzyme at pH 6.0 and 40C
14.95
Q1J0Z5
pH 7.6, 40C
18.5
B6E9W1
purified enzyme, at 37C
80
-
45C, pH 6.0
133.5
-
purified recombinant enzyme, pH 9.0, 45C
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
-
both the free and the immobilized enzyme exhibit an optimal reaction pH of 6.0
6.5
B1PK99
-
6.5
B1PK99
assay at
6.5
Q5SL15
assay at
6.5
-
free enzyme
7
A8QX00
in 100 mM phosphate buffer
7
-
both free and chitosan-immobilized enzymes
7
-
at 35C in Na-phosphate buffer
7
-
spherical aggregated enzyme
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
Q9RST7
activity range, profile, overview
5 - 10
-
over 50% of maximal activity within this range
5 - 7
-
pH 5: about 25% of maximal activity, pH 7: about 55% of maximal activity
5 - 7.5
-
more than 80% of maximum activity within this range
5 - 8
-
free and spherical aggregated enzyme
6 - 7
B1PK99
-
6.5 - 9
-
more than 80% of activity is maintained from pH 6.5 and 7.5, the activities of the enzyme markedly decrease in 50 mM Tris-HCl buffer from pH 7.0-9.0
6.8 - 8.8
Q1J0Z5
more than 80% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
maximal yield of trehalulose from sucrose
40
-
fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus
40
Q7WUI5
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
40
A8QX00
in 100 mM phosphate buffer
40
-
immobilized enzyme
45
-
free enzyme
50
B1PK99
recombinant wild-type enzyme and mutant TSMrTt
53
-
free enzyme
60
Q5SL15
recombinant wild-type enzyme and mutant TSTtMr
65
Q7WUI5
wild-type
70 - 80
-
both free and chitosan-immobilized enzymes
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
70
-
spherical aggregated enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 50
Q9RST7
activity range, profile, overview
15 - 55
-
over 30% of maximal activity within this range
25 - 55
Q1J0Z5
more than 80% of maximum activity
40 - 70
-
free enzyme
50 - 80
-
spherical aggregated enzyme
50
-
at 50C a higher relative activity, 88.8%, is observed for the immobilized enzyme, compared to 76.92% for the free enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
calculated
4.9
Q1J0Z5
calculated
4.94
Q9RST7
sequence calculation
PDB
SCOP
CATH
ORGANISM
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61800
B6E9W1
predicted from amino acid sequence
705534
65000
B6E9W1
His-tagged enzyme, SDS-PAGE
705534
68000
B8YM30
SDS-PAGE
701844
110000
B1PK99
SDS-PAGE
703606
126900
Q9RST7
recombinant His6-tagged enzyme, gel filtration
726558
132300
Q1J0Z5
gel filtration, recombinant protein
718530
250000
-
gel filtration
3493
390000
-
gel filtration
692302
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 110000, calculation from nucleotide sequence
?
-
x * 105000, SDS-PAGE
?
-
x * 65000, SDS-PAGE
?
-
x * 75000
?
-
x * 106000, SDS-PAGE of recombinant enzyme, x * 164000, SDS-PAGE of recombinant fusion protein beta-amylase of Clostridium thermofluorogenes and trehalose synthase
?
Q7WUI5
x * 106000, wild-type, x * 61000, deletion mutant lacking 415 amino acids from C-terminus, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 60700, wild-type, calculated, x * 61000, wild-type, SDS-PAGE, x * 106000, fusion protein of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, SDS-PAGE
?
-
x * 70000, calculated from amino acid sequence
?
-
x * 63300, about, sequence calculation
?
-
x * 68202, sequence calculation, x * 65237, mass spectrometry
?
Pseudomonas putida P06
-
x * 75000
-
?
Corynebacterium glutamicum ATCC13032
-
x * 70000, calculated from amino acid sequence
-
dimer
A0R6E0
2 * 68000, SDS-PAGE
dimer
Q1J0Z5
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
dimer
Deinococcus geothermalis 11300
-
x * 63620, calculated, x * 6400, SDS-PAGE of recombinant protein
-
dimer
Mycobacterium smegmatis ATCC 700084
-
2 * 68000, SDS-PAGE
-
homodimer
Q9RST7
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
homodimer
Deinococcus radiodurans DSMZ 20539
-
2 * 62710, sequence calculation, 2 * 64690, recombinant His6-tagged enzyme, sequence calculation, 2 * 64000, recombinant His6-tagged enzyme, SDS-PAGE
-
homohexamer
-
6 * 65000, SDS-PAGE
tetramer
-
4 * 67000, SDS-PAGE
tetramer
-
4 * 67000, SDS-PAGE
-
homohexamer
-
6 * 68000, gel filtration
additional information
A0R6E0
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
additional information
Q5SL15
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
B1PK99
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
additional information
Meiothermus ruber CBS-01
-
the isolated N-terminal domain from Meiothermus ruber is not active. The secondary structure of the isolated N-terminal domain undergoes a greater change than that of the isolated C-terminus, three-dimensional structure enzyme structure analysis and molecular modeling, overview
-
additional information
Mycobacterium smegmatis ATCC 700084
-
determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free enzyme and enzyme in complex with inhibitor acarbose, hanging drop vapor diffusion technique, mixing of 0.002 ml of 20 mg/ml protein in 40 mM sodium phosphate buffer, pH 6.0, with 0.002 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 6.5, 0.2 M MgCl2, and 10-14% PEG 1000, 20C, 1 day to 1 week, X-ray diffraction structure determination and analysis at 1.84 A resolution, molecular replacement
A0R6E0
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
B1PK99
the enzyme can maintain very high activity (above 90%) at pH 4.0-8.0 for 5 h, below pH 5.0 the enzyme shows no activity
703606
4
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 30C, inactivation
726558
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
5 - 8.5
-
-
715078
5.5 - 7.5
B8YM30
-
701844
5.5 - 8
-
wild-type
680304
5.5 - 9.5
-
60C, 60 min, stable
3489
5.5
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 30C, 50% activity remaining
726558
6 - 9
-
20C, 60 min, stable
3490
6 - 9
Q7WUI5
-
680304
6.5 - 8
-
the enzyme activity declines significantly at pH above 6.5. At pH 8.0 a complete loss in enzyme activity is observed for both the free and the immobilized enzyme. At pH5.0, the immobilized enzyme exhibits a relative activity, 82.13%, higher than the free enzyme, 50.57%.
716805
6.6 - 7.4
-
30 min, more than 80% residual activity
681153
7 - 9
-
37C, 1 h, stable
3493
7.6
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 45C and pH 7.6, stable
726558
9.5
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 30C, 50% activity remaining
726558
10
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 30C, inactivation
726558
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
pH 7.0, 60 min, stable up to
3490
35
-
60 min, more than 80% residual activity
681153
40 - 60
B8YM30
the enzyme remains stable up to 40C, and shows complete loss of activity at 60C
701844
40
-
30 min, more than 80% residual activity
681153
40
-
about 80% of activity is retained at 40C, but the enzyme is not stable at higher temperature than 40C
715078
40
Q1J0Z5
half-life 42 h
718530
45
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, 45C and pH 7.6, stable up to
726558
50
Q9RST7
purified recombinant His6-tagged enzyme, 2 h, pH 7.6, inactivation; purified recombinant His6-tagged enzyme, 8 h, pH 7.6, 56% activity remaining
726558
55
-
pH 7.0, 1 h, stable below
3493
55
Q1J0Z5
8 h, 57% residual activity
718530
60
-
pH 6.0, stable for 20 min
680282
60
-
30 min, wild-type, almost complete loss of activity, fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus, 83% residual activity
680304
60
B1PK99
the enzyme maintains very high activity (above 90%) at 60C for 5 h
703606
60
Q1J0Z5
2 h, 20% residual activity
718530
65
-
the wild type enzyme retains 40% of activity after 120 min at 65C
715072
70 - 80
-
the half-life of heat inactivation for free and chitosan-immobilized enzymes is 5.7 and 6.3 days at 70C, respectively. The free enzyme displays complete loss of activity after 8 days at 80C, whereas the chitosan-immobilized enzyme still retains about 25% of the initial activity
705096
70
B1PK99
half-lives of purified wild-type enzyme: 48.5 min, purified mutant TSMrTt : 47.6 min, and purified mutant TSTtMr: over 480 min, mutant R392A: 42.2 min
727433
70
Q5SL15
half-lives of purified wild-type enzyme: over 480 min, purified mutant TSMrTt : 47.6 min, and purified mutant TSTtMr: over 480 min
727433
75
B1PK99
half-lives of purified wild-type enzyme: 15.8 min, purified mutant TSMrTt : 17.6 min, and purified mutant TSTtMr: over 480 min, mutant R392A: 12.5 min
727433
75
Q5SL15
half-lives of purified wild-type enzyme: 475 min, purified mutant TSMrTt : 17.6 min, and purified mutant TSTtMr: over 480 min
727433
80
-
pH 7.0, 60 min, stable up to
3489
80
Q7WUI5
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
680304
80
B1PK99
half-lives of purified wild-type enzyme: below 5 min, purified mutant TSMrTt : below 5 min, and purified mutant TSTtMr: 27.6 min, mutant R392A: below 5 min
727433
80
Q5SL15
half-lives of purified wild-type enzyme: 233 min, purified mutant TSMrTt : below 5 min, and purified mutant TSTtMr: 27.6 min
727433
100
B1PK99
purified enzyme, 10 min, inactivation
727433
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme immobilized with highly porous cross-linked polystyrene divinylbezene-based metal chelator maintains a residual activity of ca. 80% after 24 cycles
-
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
4C, 150 days, retains 82% of its initial activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
A8QX00
Ni-NTA column chromatography
B8YM30
Ni-NTA column chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain (DE3) Rosetta pLysS by cobalt affinity chromatography and ultrafiltration
Q9RST7
Ni-NTAcolumn chromatography
B6E9W1
Ni-NTA column chromatography
B1PK99
recombinant His6-tagged wild-type and chimeric mutant enzymes from Escherichia coli strain Rosetta-gami (DE3) by nickel affinity chromatography
B1PK99
Ni column chromatography, DEAE-cellulose column chromatography, hydroxyapatite column chromatography, aminohexylagarose column chromatography, phenyl-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Ni column chromatography
-
HiTrap Chelating HP column chromatography
-
recombinant enzyme
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant enzyme
-
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
Q5SL15
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
A8QX00
expressed in Escherichia coli BL21(DE3) cells
B8YM30
expressed in Escherichia coli MC1061 cells
-
expression in Escherichia coli
Q1J0Z5
expression in Escherichia coli
-
locus DR-2036, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of C-terminally His6-tagged enzyme in Escherichia coli strain (DE3) Rosetta pLysS from pET30Ek/LIC vector
Q9RST7
expressed in Escherichia coli BL21(DE3) cells
B6E9W1
expressed in Escherichia coli Rosetta gami (DE3) cells
B1PK99
gene treS, sequence comparison, expression of His6-tagged wild-type enzyme and the chimeric mutant in Escherichia coli strain Rosetta-gami (DE3), subcloning in Escherichia coli strain DH5alpha
B1PK99
recombinant expression in Escherichia coli
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expressed in Escherichia coli Rosetta-gami B cells
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expression in Escherichia coli
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recombinant expression in two plasmid-bearing Escherichia coli strains BL21(DE3)/pET23a(+)-PTTS and Rosetta(DE3)/pET23a(+)-PTTS, optimized expression in Escherichia coli strains BT04-BT06 with deleted genes treA or treF or both, which encode for trehalases, overview; strategy for stable and high-level expression of recombinant trehalose synthase in Escherichia coli
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gene treS, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli
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construction of fusion genes from beta-amylase gene of Clostridium thermofluorogenes and trehalose synthase and overexpression in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
Q7WUI5
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
Q5SL15
gene treS, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic tree, recombinant overexression in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain D5alpha
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression induction with 0.4 mM IPTG at 25C for 5 h is the best condition for the expression of soluble TreS, higher temperature or IPTG concentrations lead to a higher rate of inclusion bodies, whereas a temperature below 20C and lower IPTG concentrations decreases the total amount of TreS
B8YM30
expression induction with 0.4 mM IPTG at 25C for 5 h is the best condition for the expression of soluble TreS, higher temperature or IPTG concentrations lead to a higher rate of inclusion bodies, whereas a temperature below 20C and lower IPTG concentrations decreases the total amount of TreS
Arthrobacter aurescens CGMCC 1.1892
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R392A
B1PK99
site-directed mutagenesis, the mutant shows a sharp decrease in activity compared to the wild-type enzyme
R392A
Meiothermus ruber CBS-01
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site-directed mutagenesis, the mutant shows a sharp decrease in activity compared to the wild-type enzyme
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R392F
Meiothermus ruber CBS-01
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site-directed mutagenesis, the mutation leads to a complete loss in activity
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A255P
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2.0% activity compared to the wild type enzyme
D411P
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3.2% activity compared to the wild type enzyme
D41P
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99.6% activity compared to the wild type enzyme
E469P
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50% activity compared to the wild type enzyme
I121P
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21.3% activity compared to the wild type enzyme
I385P
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5.1% activity compared to the wild type enzyme
K332P
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96.7% activity compared to the wild type enzyme
N503P
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the mutant shows about 39% higher relative activity than that of the wild type at 65C for 120 min. The trehalose yield of the mutant is 1.3fold higher than that of the wild type with sweet potato starch as substrate at 50C for 4 h
R523P
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90.8% activity compared to the wild type enzyme
S439P
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20.8% activity compared to the wild type enzyme
D112A
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site-directed mutagenesis, inactive mutant
D294A
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site-directed mutagenesis, inactive mutant
D403A
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site-directed mutagenesis, inactive mutant
E338A
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site-directed mutagenesis, inactive mutant
F115A
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site-directed mutagenesis, inactive mutant
F223A
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site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
F255A
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site-directed mutagenesis, inactive mutant
Q259A
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site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
R535A
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site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
D112A
Pseudomonas putida P06
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site-directed mutagenesis, inactive mutant
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D403A
Pseudomonas putida P06
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site-directed mutagenesis, inactive mutant
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E338A
Pseudomonas putida P06
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site-directed mutagenesis, inactive mutant
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F115A
Pseudomonas putida P06
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site-directed mutagenesis, inactive mutant
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F223A
Pseudomonas putida P06
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site-directed mutagenesis, the mutation only modestly affects the enzymatic activity
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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
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fusion protein consisting of Deinococcus radiodurans enzyme N-terminus plus Thermus thermophilus enzyme C-terminus has a higher thermostability than Deinococcus radiodurans wild-type and less byproducts
additional information
B1PK99
construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
additional information
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preparation of cross-linked enzyme aggregates in a water-in-oil emulsion, spherical aggregates of recombinant trehalose synthase are obtained through the emulsion based process, method development and evaluation
R392F
B1PK99
site-directed mutagenesis, the mutation leads to a complete loss in activity
additional information
Meiothermus ruber CBS-01
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construction of a chimeric enzyme mutant consisting of the C-terminus from Meiothermus ruber trehalose synthase and the N-terminus from Thermus thermophilus trehalose synthase, TSMrTt , and a second with N-terminus from Meiothermus ruber trehalose synthase and C-terminus from Thermus thermophilus trehalose synthase, TSTtMr
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synthesis
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usage of the enzyme in a sugar nucleotide cycling process for synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, coupled reaction of trehalose synthase from Pyrococcus horikoshii with UDP-Glc 4-epimerase from Pyrococcus horikoshii, and several alpha-galactosyltransferases, method development and evaluation, overview
additional information
Q7WUI5
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
Q5SL15
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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the enzyme is useful in the biotransformation process for inexpensive production of trehalose from maltose
medicine
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trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal. The alpha-Gal epitope III with galactulose acceptor shows the most inhibitory activity of anti-adhesion of Escherichia coli cells to human Caco-2 cells. The alpha-galactosyl oligosaccharides may be alternative anti-adhesion molecules that overcome antibiotic resistance
synthesis
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trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, method development and evaluation, overview
synthesis
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immobilization of recombinant enzyme on Eupergit C250L for the production of trehalose. Immobilization does not affect optimum pH value, optimum temperature is shifted from 45C to 65C. Immobilized enzyme is stable at 70C for 16 days and can be used more than 10times in batch reaction. A maximum yield of 42% trehalose can be reached from 50 g/l maltose
synthesis
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the enzyme is a good candidate in the large-scale production of trehalose from maltose