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Literature summary extracted from

  • Jennewein, S.; Schuermann, M.; Wolberg, M.; Hilker, I.; Luiten, R.; Wubbolts, M.; Mink, D.
    Directed evolution of an industrial biocatalyst: 2-deoxy-D-ribose 5-phosphate aldolase (2006), Biotechnol. J., 1, 537-548.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.4 expressed in Escherichia coli strain BL21 Star (DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.4 D84G/DELTAY259 the catalytic activity towards 2-deoxy-D-ribose-5-phosphate cleavage is increased 4fold compared to the wild type enzyme Escherichia coli
4.1.2.4 F200I shows a nearly 14fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 K13C shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 M185T shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 M185V mutation results in an about 5fold increase in (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation compared to the wild type enzyme Escherichia coli
4.1.2.4 N80S/E127G/M185V/S258T/Y259T contains an additional C-terminal KTQLSCTKW sequence, the catalytic activity towards 2-deoxy-D-ribose-5-phosphate cleavage is increased 2.5fold compared to the wild type enzyme Escherichia coli
4.1.2.4 S239C shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 S93G/A174V shows a nearly 3fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 T19I/I166T shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli
4.1.2.4 T19S shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.4 Chloroacetaldehyde the enzyme is rapidly and irreversibly inactivated and loses 84.9% of its enzymatic activity in the presence of 200 mM chloroacetaldehyde Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.4 24
-
 Chloroacetaldehyde mutant enzyme F200I Escherichia coli
4.1.2.4 54.6
-
 Chloroacetaldehyde wild type enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.4 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.4 (S)-4-chloro-3-hydroxybutanal + acetaldehyde
-
 Escherichia coli (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside
-
 ?
4.1.2.4 2-deoxy-D-ribose 5-phosphate
-
 Escherichia coli D-glyceraldehyde 3-phosphate + acetaldehyde
-
 r
4.1.2.4 chloroacetaldehyde + acetaldehyde
-
 Escherichia coli (S)-4-chloro-3-hydroxybutanal
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.2.4 2-deoxy-D-ribose 5-phosphate aldolase
-
 Escherichia coli
4.1.2.4 DERA
-
 Escherichia coli