5.1.3.30: D-psicose 3-epimerase
This is an abbreviated version!
For detailed information about D-psicose 3-epimerase, go to the full flat file.
Word Map on EC 5.1.3.30
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5.1.3.30
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d-fructose
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tumefaciens
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agrobacterium
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d-tagatose
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d-allulose
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clostridium
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bioconversion
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synthesis
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epimerization
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metal-dependent
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ruminococcus
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cellulolyticum
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low-calorie
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ketose
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sweetener
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reusable
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d-sorbose
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izumoring
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ketohexose
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ni-affinity
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food-grade
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low-energy
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reusability
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noncharacterized
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bolteae
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fermentor
- 5.1.3.30
- d-fructose
- tumefaciens
- agrobacterium
- d-tagatose
- d-allulose
- clostridium
-
bioconversion
- synthesis
-
epimerization
-
metal-dependent
- ruminococcus
- cellulolyticum
-
low-calorie
-
ketose
-
sweetener
-
reusable
- d-sorbose
-
izumoring
-
ketohexose
-
ni-affinity
-
food-grade
-
low-energy
-
reusability
-
noncharacterized
- bolteae
-
fermentor
Reaction
Synonyms
ACL75304 protein, CB-DPEase, Ccel_0941, Clo1100_1157, CLOBOL_00069, CLOSCI_02528, Dosp-DPEase, DPE, DPEase, DTEase, RDPE, Trpr-DPEase
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Metals Ions
Metals Ions on EC 5.1.3.30 - D-psicose 3-epimerase
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Co2+
Fe2+
Mg2+
Mn2+
Ni2+
additional information
the metal-dependent enzyme requires Co2+ as optimum cofactor. The relative activity is linearly increased when adding Co2+ from 0.005 mM to 0.035 mM. When adding greater concentrations of Co2+, the relative activity tends to be stable. The optimum Co2+ concentration is 0.2 mM for catalytic activity
Co2+
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the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+
Co2+
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best metal cofactor, has no effect on pH stability and slightly imporves temperature
Co2+
metalloprotein that exhibits the highest activity in the presence of Co2+
Co2+
activates most highly at 0.5 mM, 80% of maximal activation at 1-5 mM, best divalent cation, dependent on
Co2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+
Co2+
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highly activating at 1 mM, essential for the activity of the recombinant enzyme
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the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Fe2+ the enzyme activity is reduced to 49% of that in the presence of Co2+
Fe2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Fe2+ the enzyme activity is reduced to 67% of that in presence of Co2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Mg2+ the enzyme activity is reduced to 22% of that in presence of Co2+
Mg2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Mg2+ the enzyme activity is reduced to 38% of that in presence of Co2+
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 66% of that in presence of Co2+
Mn2+
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the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 80% of that in the presence of Co2+
Mn2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Mn2+ the enzyme activity is reduced to 92% of that in presence of Co2+
Mn2+
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activates the recombinant free and immobilized enzyme, but does not affect the reaction equilibrium for both the free and the immobilized enzyme
Mn2+
the enzyme is strictly metal-dependent and requires Mn2+ as optimum cofactor for activity
the metal-dependent enzyme requires Co2+ as optimum cofactor. When Co2+ is replaced with Ni2+ the enzyme activity is reduced to 31% of that in presence of Co2+
Ni2+
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the enzyme is strictly metal-dependent and displays maximum activity in the presence of Co2+. When Co2+ is replaced with Ni2+, the enzyme activity is reduced to 14% of that in the presence of Co2+
Ni2+
the enzyme is strictly metal-dependent and shows a maximal activity in the presence of Co2+. When Co2+ is replaced with Ni2+ the enzyme activity is reduced to 65% of that in presence of Co2+
additional information
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metal-dependent enzyme, no activity without presence of divalent metal ion
additional information
the CB-DPEase is a metalloprotein, that is inactive in absence of divalent metal ions
additional information
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the CB-DPEase is a metalloprotein, that is inactive in absence of divalent metal ions
additional information
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activity is not dependent on the presence of metal ions