Literature summary for 5.1.3.30 extracted from

Zhang, W.; Li, H.; Jiang, B.; Zhang, T.; Mu, W.
Production of D-allulose from D-glucose by Escherichia coli transformant cells co-expressing D-glucose isomerase and D-psicose 3-epimerase genes (2017), J. Sci. Food. Agric., 97, 3420-3426 .

Search for more literature for 5.1.3.30

Cloned(Commentary)

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

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

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

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-psicose	Dorea sp. CAG:317	-	D-fructose	-	r

Organism

Organism	UniProt	Comment	Textmining
Dorea sp. CAG:317	-	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
Dosp-DPEase	-	Dorea sp. CAG:317
DPEase	-	Dorea sp. CAG:317

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
75	-	recombinant enzyme overexpressing Escherichia coli cells	Dorea sp. CAG:317

Temperature Stability [°C]

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

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

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Release 2023.1 (January 2023)