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Enzyme Nomenclature
Information on EC 5.1.3.B12 - Agrobacterium tumefaciens D-psicose 3-epimerase
for references in articles please use BRENDA:EC5.1.3.B12preliminary BRENDA-supplied EC number
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5.1.3.B12 Agrobacterium tumefaciens D-psicose 3-epimeraseSpecify your search results
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The expected taxonomic range for this enzyme is: Agrobacterium tumefaciens
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agtu
Atu4750
D-psicose-3-epimerase
DPE
DPEase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-psicose = D-fructose
-
-
-
-
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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
D-fructose
D-psicose
the catalytic efficiency of the enzyme for D-psicose is 586fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 32:68 at 30°C. D-Psicose is produced at 230 g/l from 700-g/l D-fructose at 50°C after 100 min, corresponding to a conversion yield of 32.9%
-
-
r
D-fructose
D-psicose
Agrobacterium tumefaciens ATCC 33970
the catalytic efficiency of the enzyme for D-psicose is 586fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 32:68 at 30°C. D-Psicose is produced at 230 g/l from 700-g/l D-fructose at 50°C after 100 min, corresponding to a conversion yield of 32.9%
-
-
r
D-psicose
D-fructose
the catalytic efficiency of the enzyme for D-psicose is 586fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 32:68 at 30°C. D-Psicose is produced at 230 g/l from 700-g/l D-fructose at 50°C after 100 min, corresponding to a conversion yield of 32.9%
-
-
r
D-psicose
D-fructose
Agrobacterium tumefaciens ATCC 33970
the catalytic efficiency of the enzyme for D-psicose is 586fold higher than that for D-tagatose. The equilibrium ratio between D-psicose and D-fructose is 32:68 at 30°C. D-Psicose is produced at 230 g/l from 700-g/l D-fructose at 50°C after 100 min, corresponding to a conversion yield of 32.9%
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r
additional information
?
-
no activity on D-fructose-6-phosphate or D-ribulose-5-phosphate
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-
?
additional information
?
-
-
no activity on D-fructose-6-phosphate or D-ribulose-5-phosphate
-
-
?
additional information
?
-
the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively
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-
?
additional information
?
-
Agrobacterium tumefaciens ATCC 33970
no activity on D-fructose-6-phosphate or D-ribulose-5-phosphate
-
-
?
additional information
?
-
Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970
the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively
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-
?
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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
additional information
?
-
the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively
-
-
?
additional information
?
-
Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970
the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mn2+
additional information
Co2+
1 mM, 2.7fold increase in the epimerization rate from D-fructose to D-psicose
Co2+
highly activating, addition of Mg2+ to media containing Co2+ can further improve the conversion rate by 1.24fold, while Mg2+ alone is not activating
Co2+
significantly increases the DPEase activity by 2.75fold at 1 mM compared to control
Mn2+
1 mM, 2.7fold increase in the epimerization rate from D-fructose to D-psicose
Mn2+
the distances between the catalytic residues (Glu150 and Glu244) and Mn2+ are critical to the catalysis, and the negative charges of the metal-binding residues are important for interaction with metal ion
Mn2+
activates strongly at 1 mM, even low levels of Mn2+ (0.025-0.1 mM) in the assay reaction are sufficient for enhancing the enzyme's activity
Mn2+
significantly increases the enzyme activity by 2.89fold at 1 mM compared to control
additional information
metal ion with octahedral coordination to two water molecules and four amino acid residues
additional information
Al3+, Fe2+, and Fe3+ have no effect on enzyme activity at 1 mM
additional information
-
Al3+, Fe2+, and Fe3+ have no effect on enzyme activity at 1 mM
additional information
Mg2+, Fe2+ and Ba2+ at 1 mM have no significant effct on the activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
activity of D-psicose 3-epimerase is 20% after the removal of metal ions by treatment with EDTA
Cu2+
significantly inhibits the DPEase activity by 0.1fold at 1 mM compared to control
Zn2+
significantly inhibits the DPEase activity by 0.12fold at 1 mM compared to control
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
recombinant His-tagged mutant enzyme in vivo in recombinant cells
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
60
recombinant His-tagged mutant enzyme in vivo in recombinant cells
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 70
activity range, profile overview, recombinant enzyme
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Agrobacterium tumefaciens C58 / ATCC 33970
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
high-level extracellular production of D-psicose-3-epimerase with recombinant Escherichia coli. Addition of glycine has a positive effect on the extracellular production of the enzyme
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brenda
Agrobacterium tumefaciens C58 / ATCC 33970
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high-level extracellular production of D-psicose-3-epimerase with recombinant Escherichia coli. Addition of glycine has a positive effect on the extracellular production of the enzyme
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase based on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template
additional information
Agrobacterium tumefaciens C58 / ATCC 33970
-
structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase based on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template
-
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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). DPES_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
289
0
31566
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
132000
180000
recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
?
Agrobacterium tumefaciens C58 / ATCC 33970
-
x * 33000, recombinant His-tagged mutant enzyme, SDS-PAGE
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?
Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970
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x * 32000, recombinant His-tagged enzyme, SDS-PAGE
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tetramer
4 * 45000, recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, SDS-PAGE, 4 * 33000, recombinant wild-type enzyme, SDS-PAGE
tetramer
Agrobacterium tumefaciens EHA 105 / NCIM 2942
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4 * 45000, recombinant chimeric Smt3-D-psicose 3-epimerase conjugate, SDS-PAGE, 4 * 33000, recombinant wild-type enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of DPEase and its complex with the true substrate D-fructose. Diffraction-quality crystals of native and SeMet-enzyme are grown in 14–15% (w/v) PEG 1000, 0.1 M imidazole (pH 8.0), 0.2 M calcium acetate within five days to overall dimensions of 0.4 mm * 0.28 mm * 0.28 mm
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A107I
7.7fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
A107P
1.4fold decrease in kcat/Km for D-fructose, 6.6fold decrease in kcat/Km for D-tagatose
A107V
13.9fold decrease in kcat/Km for D-fructose, no activity detected with D-tagatose
G67C
the variant shows remarkably decreased specific activity
I33L
increase of 5°C in the temperature for maximal enzyme activity, increase of 7.2-fold in the half-life at 50°C, and increase of 4.3°C in apparent melting temperature, respectively, compared with the wild-type enzyme
I33L-S213C
site-directed mutagenesis, structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template. Production of D-psicose from D-fructose by whole recombinant cells and its crude enzyme under optimized conditions, overview
I33L/S213C
increase of 7.5°C in the temperature for maximal enzyme activity, increase of 29.9-fold in the half-life at 50°C, and increase of 7.6°C in apparent melting temperature, respectively, compared with the wild-type enzyme. After 8 or 16 days, the enzyme activity gradually decreases, and the conversion yields with and without borate are reduced to 22 and 9.6%, respectively, at 30 days. In contrast, the activity of the immobilized I33L/S213C variant with and without borate does not decrease during the operation time of 30 days
I66A
1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
I66C
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
I66F
2.1fold decrease in kcat/Km for D-fructose, 23.3fold decrease in kcat/Km for D-tagatose
I66G
1.9fold decrease in kcat/Km for D-fructose, 87.5fold decrease in kcat/Km for D-tagatose
I66L
1.6fold increase in kcat/Km for D-fructose, 58,3fold decrease in kcat/Km for D-tagatose
I66V
1.9fold decrease in kcat/Km for D-fructose, 24fold decrease in kcat/Km for D-tagatose
I66W
1.4fold decrease in kcat/Km for D-fructose, 42fold decrease in kcat/Km for D-tagatose
I66Y
3fold decrease in kcat/Km for D-fructose, 26fold decrease in kcat/Km for D-tagatose
S213C
increase of 2.5°C in the temperature for maximal enzyme activity, increase of 3.3-fold in the half-life at 50°C, and increase of 3.1°C in apparent melting temperature, respectively, compared with the wild-type enzyme. Immobilized wild-type enzyme with and without borate maintains activity for 8 days at a conversion yield of 70% (350 g/l psicose) and for 16 days at a conversion yield of 30% (150 g/l psicose), respectively
W112F
mutant enzyme displays 19% of the wild type enzyme activity. kcat/Km for D-fructose is 100fold lower than wild-type value, kcat/Km fur D-psicose is 84fold lower than wild-type value
W112H
mutant enzyme displays 65% of the wild type enzyme activity
W112Y
mutant enzyme displays 54% of the wild type enzyme activity
I33L
Agrobacterium tumefaciens ATCC 33970
-
increase of 5°C in the temperature for maximal enzyme activity, increase of 7.2-fold in the half-life at 50°C, and increase of 4.3°C in apparent melting temperature, respectively, compared with the wild-type enzyme
-
I33L/S213C
Agrobacterium tumefaciens ATCC 33970
-
increase of 7.5°C in the temperature for maximal enzyme activity, increase of 29.9-fold in the half-life at 50°C, and increase of 7.6°C in apparent melting temperature, respectively, compared with the wild-type enzyme. After 8 or 16 days, the enzyme activity gradually decreases, and the conversion yields with and without borate are reduced to 22 and 9.6%, respectively, at 30 days. In contrast, the activity of the immobilized I33L/S213C variant with and without borate does not decrease during the operation time of 30 days
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I66A
Agrobacterium tumefaciens ATCC 33970
-
1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
-
I66C
Agrobacterium tumefaciens ATCC 33970
-
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
-
I66G
Agrobacterium tumefaciens ATCC 33970
-
1.9fold decrease in kcat/Km for D-fructose, 87.5fold decrease in kcat/Km for D-tagatose
-
I66L
Agrobacterium tumefaciens ATCC 33970
-
1.6fold increase in kcat/Km for D-fructose, 58,3fold decrease in kcat/Km for D-tagatose
-
I66V
Agrobacterium tumefaciens ATCC 33970
-
1.9fold decrease in kcat/Km for D-fructose, 24fold decrease in kcat/Km for D-tagatose
-
S213C
Agrobacterium tumefaciens ATCC 33970
-
increase of 2.5°C in the temperature for maximal enzyme activity, increase of 3.3-fold in the half-life at 50°C, and increase of 3.1°C in apparent melting temperature, respectively, compared with the wild-type enzyme. Immobilized wild-type enzyme with and without borate maintains activity for 8 days at a conversion yield of 70% (350 g/l psicose) and for 16 days at a conversion yield of 30% (150 g/l psicose), respectively
-
W112F
Agrobacterium tumefaciens ATCC 33970
-
mutant enzyme displays 19% of the wild type enzyme activity. kcat/Km for D-fructose is 100fold lower than wild-type value, kcat/Km fur D-psicose is 84fold lower than wild-type value
-
W112H
Agrobacterium tumefaciens ATCC 33970
-
mutant enzyme displays 65% of the wild type enzyme activity
-
W112Y
Agrobacterium tumefaciens ATCC 33970
-
mutant enzyme displays 54% of the wild type enzyme activity
-
I33L-S213C
Agrobacterium tumefaciens C58 / ATCC 33970
-
site-directed mutagenesis, structure homology modeling and substrate docking the double-site variant I33L-S213C DPEase on the crystal structure of DPEase from Agrobacterium tumefaciens, PDB Id 2HK0, as a template. Production of D-psicose from D-fructose by whole recombinant cells and its crude enzyme under optimized conditions, overview
-
additional information
additional information
for production of D-psicose from D-glucose in an enzymatic process, the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively. Co2+ is strictly required. Method optimization and evaluation, overview
additional information
immobilization of Agrobacterium tumefaciens DPEase (agtu-DPEase) on graphene oxide particles (GO-agtu-DPEase). Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Graphene oxide immobilized agtu-DPEase (GO-agtu-DPEase) shows optima at pH 7.5 and 60°C. Significant improvement in thermal stability is observed with half-life of 720 min at 60°C while unbound (agtu) DPEase is stable for 3.99 min at 60°C. At equilibrium, the bioconversion efficiency is accounted 40:60 (D-psicose: D-fructose) for graphene oxide-immobilized DPEase which is higher than for the free agtu-DPEase (32:68). Graphene oxide immobilized DPEase shows bioconversion efficiency up to 10 cycles of reusability
additional information
improved operational stability of D-psicose 3-epimerase by a protein engineering strategy by introduction of a SUMO fusion system, using Saccharomyces cerevisiae Smt3, as the N-terminal tag, which can significantly enhance operational stability and bioconversion efficiency of D-psicose 3-epimerase. The Smt3-D-psicose 3-epimerase conjugate system exhibits relatively better catalytic efficiency, and improved productivity in terms of space-time yields of about 8.5 kg/l/day, it can serve as a catalytic tool for the pilot scale production of the functional sugar, D-psicose, D-psicose production from fruit and vegetable remains and agro-industrial by-products, overview. The bioprocessing leads to achievement of D-psicose production to the extent of 25-35% conversion w/w of D-fructose contained in the sample
additional information
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
additional information
-
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
additional information
Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970
-
for production of D-psicose from D-glucose in an enzymatic process, the xylose isomerase gene from Escherichia coli strain MG1665 and the D-psicose 3-epimerase gene from Agrobacterium tumefaciens CGMCC 1.1488 are coexpressed in Escherichia coli strain BL21(DE3). After 24 h incubation with the dual enzyme system at 40°C, the sugar conversion ratio from D-glucose to D-psicose reaches 10%. The optimal conditions are 50°C, pH 7.5 with Co2+ and Mg2+. The D-psicose yields from sugarcane bagasse and microalgae hydrolysate are 1.42 and 1.69 g/L, respectively. Co2+ is strictly required. Method optimization and evaluation, overview
-
additional information
Agrobacterium tumefaciens EHA 105 / NCIM 2942
-
improved operational stability of D-psicose 3-epimerase by a protein engineering strategy by introduction of a SUMO fusion system, using Saccharomyces cerevisiae Smt3, as the N-terminal tag, which can significantly enhance operational stability and bioconversion efficiency of D-psicose 3-epimerase. The Smt3-D-psicose 3-epimerase conjugate system exhibits relatively better catalytic efficiency, and improved productivity in terms of space-time yields of about 8.5 kg/l/day, it can serve as a catalytic tool for the pilot scale production of the functional sugar, D-psicose, D-psicose production from fruit and vegetable remains and agro-industrial by-products, overview. The bioprocessing leads to achievement of D-psicose production to the extent of 25-35% conversion w/w of D-fructose contained in the sample
-
additional information
Agrobacterium tumefaciens EHA 105 / NCIM 2942
-
the engineered Kluyveromyces marxianus strain CICC1911 expressing gene dpe produces 190 g/l D-allulose with 750 g/l D-fructose as a substrate at 55°C within 12 h. Approximately 100 g of residual D-fructose are converted into 34 g of ethanol, and 15 g of the engineered Kluyveromyces marxianus cells are regenerated after fermentation at 37°C for 21 h. A purity of D-allulose of more than 90% can be obtained without isolating it from D-allulose and D-fructose mixture through residual D-fructose consumption, method development and evaluation of a valuable pathway to regenerate engineered cells and achieve cyclic catalysis for D-allulose production, overview
-
additional information
Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970
-
immobilization of Agrobacterium tumefaciens DPEase (agtu-DPEase) on graphene oxide particles (GO-agtu-DPEase). Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production. Graphene oxide immobilized agtu-DPEase (GO-agtu-DPEase) shows optima at pH 7.5 and 60°C. Significant improvement in thermal stability is observed with half-life of 720 min at 60°C while unbound (agtu) DPEase is stable for 3.99 min at 60°C. At equilibrium, the bioconversion efficiency is accounted 40:60 (D-psicose: D-fructose) for graphene oxide-immobilized DPEase which is higher than for the free agtu-DPEase (32:68). Graphene oxide immobilized DPEase shows bioconversion efficiency up to 10 cycles of reusability
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
purified recombinant chimeric enzyme, retains about 80% of the initial activity after 5 h, completely stable at pH 8.0
747298
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50 - 55
half-lives of whole recombinant cells at 50°C and 55°C are 125 and 177% higher than those of its double-site variant enzyme, respectively. The thermostability of whole cells is higher than that of enzyme
55
60
50
the wild-type, S213C, I33L, and I33L S213C variant enzymes have half-lives of 62, 202, 445, and 1,853 min at 50°C, respectively
50
purified recombinant chimeric enzyme, retains 45% of the initial activity after 12 h
55
half-life of wild-type enzyme: 10 min, half-lives of mutant enzymes: G67C (132 min), I33L (64 min), S213C (28 min), V96A (18 min), S8T (15 min), S213P (6 min), S213T (5 min), S213M (3.2 min), S213E (2.8 min)
60
graphene oxide-immobilized enzyme DPEase has a half-life of 720 min, while unbound (agtu) DPEase is stable for 3.99 min
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant engineered Smt3-D-psicose 3-epimerase conjugate from Escherichia coli strain BL21 by nickel affinity and anion exchange chromatography
recombinant enzyme from Kluyveromyces marxianus strain CICC1911 by ammonium sulfate fractionation and nickel affinity chromatography
recombinant His-tagged enzyme from Agrobacterium tumefaciens by nickel affinity chromatography, and dialysis
recombinant His6-tagged enzyme 1.59fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of the D-psicose 3-epimerase gene, recombinant expression in Escherichia coli strain BL21(DE3), co-expression with xylose isomerase gene from Escherichia coli strain MG1665 from plasmid pET-28a-DPE-xylA
expression in Escherichia coli. It has no significant sequence similarities to D-tagatose 3-epimerase. It is genetically different from other sugar epimerases
gene agtu, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene agtu, subcloning in Escherichia coli strain ER2566, expression of recombinant His-tagged enzyme mutant I33L-S213C in Agrobacterium tumefaciens at high level, optimal at optimal at 60x02C, pH 8.5, 4 g/l cells, and 700 g/l D-fructose. The recombinant cells produced 230 g/l D-psicose after 40 min, with a conversion yield of 33% w/w, a volumetric productivity of 345 g/l/h, and a specific productivity of 86.2 g/g/h
gene dpe, DNA and amino acid sequence determination and analysis, recombinant expression of the engineered chimeric Smt3-D-psicose 3-epimerase conjugate in Escherichia coli strain BL21
gene dpe, functional recombinant expression of the enzyme in thermotolerant Kluyveromyces marxianus strain CICC1911, pRS42H-dpe is transformed into the thermotolerant cells of strain CICC1911 by using the LiAc/salmon sperm carrier DNA/PEG method
the gene AAL45544.1 from Agrobacterium tumefaciens str. C58 is modified by artificial synthesis for overexpression in Escherichial coli, expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
synthesis
medicine
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
medicine
Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970
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D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
-
nutrition
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
nutrition
Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970
-
D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar. It is regarded as a low calorie sweetener, an inhibitor of hepatic lipogenic enzymes, an activator of abdominal lipolysis and intestinal alpha-glycosidase enzymes D-psicose reduces the hyperglycemia, obesity, and hyperlipidemia and decrease the blood glucose level in type-2 diabetes
-
synthesis
the enzyme can be used for synthesis of D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar
synthesis
the enzyme from Agrobacterium tumefaciens can be used for production of D-psicose in a coexpression system with xylose isomerase gene from Escherichia coli. Method optimization and evaluation, overview
synthesis
Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970
-
the enzyme can be used for synthesis of D-psicose (D-ribo-2-hexulose or D-allulose), a C3 epimer of D-fructose and considered as a rare sugar
-
synthesis
Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970
-
the enzyme from Agrobacterium tumefaciens can be used for production of D-psicose in a coexpression system with xylose isomerase gene from Escherichia coli. Method optimization and evaluation, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, H.J.; Hyun, E.K.; Kim, Y.S.; Lee, Y.J.; Oh, D.K.
Characterization of an Agrobacterium tumefaciens D-psicose 3-epimerase that converts D-fructose to D-psicose
Appl. Environ. Microbiol.
72
981-985
2006
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens, Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Choi, J.G.; Ju, Y.H.; Yeom, S.J.; Oh, D.K.
Improvement in the thermostability of D-psicose 3-epimerase from Agrobacterium tumefaciens by random and site-directed mutagenesis
Appl. Environ. Microbiol.
77
7316-7320
2011
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Gu, L.; Zhang, J.; Liu, B.; Wu, C.; Du, G.; Chen, J.
High-level extracellular production of D-psicose-3-epimerase with recombinant Escherichia coli by a two-stage glycerol feeding approach
Bioprocess Biosyst. Eng.
36
1767-1777
2013
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
brenda
Kim, H.J.; Lim, B.C.; Yeom, S.J.; Kim, Y.S.; Kim, D.; Oh, D.K.
Roles of Ile66 and Ala107 of D-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, D-fructose
Biotechnol. Lett.
32
113-118
2009
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Kim, H.J.; Yeom, S.J.; Kim, K.; Rhee, S.; Kim, D.; Oh, D.K.
Mutational analysis of the active site residues of a D-psicose 3-epimerase from Agrobacterium tumefaciens
Biotechnol. Lett.
32
261-268
2010
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Kim, K.; Kim, H.J.; Oh, D.K.; Cha, S.S.; Rhee, S.
Crystal structure of D-psicose 3-epimerase from Agrobacterium tumefaciens and its complex with true substrate D-fructose: a pivotal role of metal in catalysis, an active site for the non-phosphorylated substrate, and its conformational changes
J. Mol. Biol.
361
920-931
2006
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens ATCC 33970 (A9CH28)
brenda
Patel, S.N.; Sharma, M.; Lata, K.; Singh, U.; Kumar, V.; Sangwan, R.S.; Singh, S.P.
Improved operational stability of D-psicose 3-epimerase by a novel protein engineering strategy, and D-psicose production from fruit and vegetable residues
Biores. Technol.
216
121-127
2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens EHA 105 / NCIM 2942 (A9CH28)
brenda
Chen, X.; Wang, W.; Xu, J.; Yuan, Z.; Yuan, T.; Zhang, Y.; Liang, C.; He, M.; Guo, Y.
Production of D-psicose from D-glucose by co-expression of D-psicose 3-epimerase and xylose isomerase
Enzyme Microb. Technol.
105
18-23
2017
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens CGMCC 1.1488 / C58 / ATCC 33970 (A9CH28)
brenda
Dedania, S.R.; Patel, M.J.; Patel, D.M.; Akhani, R.C.; Patel, D.H.
Immobilization on graphene oxide improves the thermal stability and bioconversion efficiency of D-psicose 3-epimerase for rare sugar production
Enzyme Microb. Technol.
107
49-56
2017
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens MTCC 609 / C58 / ATCC 33970 (A9CH28)
brenda
Park, C.S.; Park, C.S.; Shin, K.C.; Oh, D.K.
Production of d-psicose from D-fructose by whole recombinant cells with high-level expression of D-psicose 3-epimerase from Agrobacterium tumefaciens
J. Biosci. Bioeng.
121
186-190
2016
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens C58 / ATCC 33970 (A9CH28)
brenda
Yang, P.; Zhu, X.; Zheng, Z.; Mu, D.; Jiang, S.; Luo, S.; Wu, Y.; Du, M.
Cell regeneration and cyclic catalysis of engineered Kluyveromyces marxianus of a D-psicose-3-epimerase gene from Agrobacterium tumefaciens for D-allulose production
World J. Microbiol. Biotechnol.
34
65
2018
Agrobacterium tumefaciens (A9CH28), Agrobacterium tumefaciens, Agrobacterium tumefaciens EHA 105 / NCIM 2942 (A9CH28)
brenda
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