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Literature summary for 4.1.2.4 extracted from

  • Fei, H.; Xu, G.; Wu, J.; Yang, L.
    Improvement of the thermal stability and aldehyde tolerance of deoxyriboaldolase via immobilization on nano-magnet material (2014), J. Mol. Catal. B, 101, 87-91 .
No PubMed abstract available
Search for more literature for 4.1.2.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(pET30) Escherichia coli

General Stability

General Stability Organism
the immobilized enzyme is highly resistant to acetaldehyde. The enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material retains 67.4% of its 2-deoxy-D-ribose-5-phosphate cleavage activity after incubation for 10 h in the presence of 300 mM acetaldehyde at 25°C. No activity is observed for the free enzyme after incubation for 3 h under the same conditions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Storage Stability

Storage Stability Organism
4°C, 80 days, the residual activity of the enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material, and of the enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material, is 77.5%, 1.85 times better than that of the soluble enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-ribose 5-phosphate
-
 Escherichia coli D-glyceraldehyde 3-phosphate + acetaldehyde
-
 ?

Synonyms

Synonyms Comment Organism
2-deoxy-D-ribose-5-phosphate aldolase
-
 Escherichia coli
DERA
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 70 30°C: about 50% of maximal activity, 70°C: about 40% of maximal activity, soluble enzyme Escherichia coli
30 85 30°C: about 55% of maximal activity, 85°C: about 50% of maximal activity, enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
 the enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilanenano-magnet material exhibits a wider range of reaction temperatures than the free enzyme Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 10 min, the enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnetmaterial possesses 65.7% of its initial activity after incubation, the soluble enzyme loses almost all of its activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 cleavage of 2-deoxy-D-ribose 5-phosphate, soluble enzyme Escherichia coli
8
-
 cleavage of 2-deoxy-D-ribose 5-phosphate, enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6 10.5 pH 6.0: about 50% of maximal activity, pH 10.5: about 40% of maximal activity, soluble enzyme Escherichia coli
6 11.5 pH 6.0: about 50% of maximal activity, pH 11.5: about 45% of maximal activity, enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 11.5 immobilized enzyme loses very little activity at pH values ranging from 5.5 to 11.5 Escherichia coli
10
-
 soluble enzyme loses activity at pH values greater than 10.0 Escherichia coli