Literature summary for 4.1.2.4 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.

Search for more literature for 4.1.2.4

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
D84G/DELTAY259	the catalytic activity towards 2-deoxy-D-ribose-5-phosphate cleavage is increased 4fold compared to the wild type enzyme	Escherichia coli
F200I	shows a nearly 14fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
K13C	shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
M185T	shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
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
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
S239C	shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
S93G/A174V	shows a nearly 3fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
T19I/I166T	shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli
T19S	shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
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]

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

Synonyms

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

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Release 2023.1 (January 2023)