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Literature summary for 4.1.2.4 extracted from

  • Subrizi, F.; Crucianelli, M.; Grossi, V.; Passacantando, M.; Botta, G.; Antiochia, R.; Saladino, R.
    Versatile and efficient immobilization of 2-deoxyribose-5-phosphate aldolase (DERA) on multiwalled carbon nanotubes (2014), ACS Catal., 4, 3059-3068 .
No PubMed abstract available

General Stability

General Stability Organism
the enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes is stable with a high tolerance to acetaldehyde, and maintains its activity for several days, being reused for five runs Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.34
-
2-deoxy-D-ribose 5-phosphate pH 7.5, 25°C, enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes Escherichia coli
0.55
-
2-deoxy-D-ribose 5-phosphate pH 7.5, 25°C, soluble enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L0
-
-

Storage Stability

Storage Stability Organism
25°C, up to 15 days, the enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes retains almost the full activity. The soluble enzyme shows a decrease of activity after the first 5 days, thereby reaching a value of ca. 80% of residual activity after 15 days 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
-
?
acetaldehyde + acetaldehyde enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes catalyzes the reaction of acetaldehyde alone (self-condensation) or in the presence of chloro-acetaldehyde. The corresponding cyclic lactols are obtained in higher yield than with the native enzyme Escherichia coli ?
-
?
chloroacetaldehyde + acetaldehyde enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes catalyzes the reaction of acetaldehyde alone (self-condensation) or in the presence of chloro-acetaldehyde. The corresponding cyclic lactols are obtained in higher yield than with the native enzyme Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
2-Deoxyribose-5-phosphate aldolase
-
Escherichia coli
DERA
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli