Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli strain BL21(DE3), co-expression with D-glucose isomerase (GIase) from Acidothermus cellulolyticus from plasmid pETDuet-Dosp-DPE/Acce-GI | Dorea sp. CAG:317 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | on the basis of the Izumoring strategy, D-allulose can be obtained from D-glucose by coupling D-glucose isomerase (GIase) and DPEase, with D-fructose as the intermediate. In this reaction system, D-fructose is firstly converted from D-glucose by GIase, and immediately isomerised to D-allulose by DPEase. Recombinant co-expression with GIase from Acidothermus cellulolyticus from plasmid pETDuet-Dosp-DPE/Acce-GI, optimization of the biotransformation consitions, method, overview. When the reactions reaches equilibrium under optimal conditions,the equilibrium ratio of D-glucose, D-fructose and D-allulose is approximately 6.5:7:3, respectively. The transformation rate is about 18%. The optimum pH of the Acce-GI/Dosp-DPE co-expression system is lower than that of the BGI/RDPE co-expression system, while the optimum temperature is higher than that of the BGI/RDPE co-expression system | Dorea sp. CAG:317 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | - |
Dorea sp. CAG:317 | |
Ca2+ | - |
Dorea sp. CAG:317 | |
Cu2+ | - |
Dorea sp. CAG:317 | |
EDTA | complete inhibition | Dorea sp. CAG:317 | |
Fe2+ | - |
Dorea sp. CAG:317 | |
Ni2+ | - |
Dorea sp. CAG:317 | |
Zn2+ | - |
Dorea sp. CAG:317 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates 10.8fold at 1 mM, best divalent cation, dependent on | Dorea sp. CAG:317 | |
Mn2+ | activates to 23.1% of the activity with Co2+ at 1 mM | Dorea sp. CAG:317 | |
additional information | no effect on activity by Mg2+ | Dorea sp. CAG:317 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-psicose | Dorea sp. CAG:317 | - |
D-fructose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Dorea sp. CAG:317 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-psicose | - |
Dorea sp. CAG:317 | D-fructose | - |
r | |
D-psicose | i.e. D-allulose | Dorea sp. CAG:317 | D-fructose | - |
r | |
additional information | when the reaction equilibrium is reached, the ratio of D-glucose, D-fructose and D-allulose is approximately 6.5:7:3, respectively | Dorea sp. CAG:317 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Dosp-DPEase | - |
Dorea sp. CAG:317 |
DPEase | - |
Dorea sp. CAG:317 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
75 | - |
recombinant enzyme overexpressing Escherichia coli cells | Dorea sp. CAG:317 |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 64.7%, activity remaining after 18 h | Dorea sp. CAG:317 |
50 | - |
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 58.4% activity remaining after 18 h | Dorea sp. CAG:317 |
60 | - |
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 15.2% activity remaining after 18 h | Dorea sp. CAG:317 |
70 | - |
recombinant enzyme in overexpressing Escherichia coli cells, pH 6.5, 9.3% activity remaining after 30 min, inactivation after 4 h | Dorea sp. CAG:317 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
wild-type enzyme | Dorea sp. CAG:317 |
6.5 | - |
recombinant enzyme overexpressing Escherichia coli cells | Dorea sp. CAG:317 |