5.1.3.B12: Agrobacterium tumefaciens D-psicose 3-epimerase
This is an abbreviated version!
For detailed information about Agrobacterium tumefaciens D-psicose 3-epimerase, go to the full flat file.
Word Map on EC 5.1.3.B12
Reaction
Synonyms
agtu, Atu4750, D-psicose-3-epimerase, DPE, DPEase
ECTree
5.1.3.B12 Agrobacterium tumefaciens D-psicose 3-epimeraseAdvanced search results
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results (Engineering
Engineering on EC 5.1.3.B12 - Agrobacterium tumefaciens D-psicose 3-epimerase
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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
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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
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I33L/S213C
Agrobacterium tumefaciens ATCC 33970
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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
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1.4fold increase in kcat/Km for D-fructose, 150fold decrease in kcat/Km for D-tagatose
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I66C
Agrobacterium tumefaciens ATCC 33970
-
3fold decrease in kcat/Km for D-fructose, 29.2fold decrease in kcat/Km for D-tagatose
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I66G
Agrobacterium tumefaciens ATCC 33970
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1.9fold decrease in kcat/Km for D-fructose, 87.5fold decrease in kcat/Km for D-tagatose
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I66L
Agrobacterium tumefaciens ATCC 33970
-
1.6fold increase in kcat/Km for D-fructose, 58,3fold decrease in kcat/Km for D-tagatose
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I66V
Agrobacterium tumefaciens ATCC 33970
-
1.9fold decrease in kcat/Km for D-fructose, 24fold decrease in kcat/Km for D-tagatose
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S213C
Agrobacterium tumefaciens ATCC 33970
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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
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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
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W112H
Agrobacterium tumefaciens ATCC 33970
-
mutant enzyme displays 65% of the wild type enzyme activity
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W112Y
Agrobacterium tumefaciens ATCC 33970
-
mutant enzyme displays 54% of the wild type enzyme activity
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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
-
