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Information on EC 4.1.2.4 - deoxyribose-phosphate aldolase and Organism(s) Escherichia coli and UniProt Accession P0A6L0
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4.1.2.4 deoxyribose-phosphate aldolaseSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
tgdpa, deoxyriboaldolase, 2-deoxyribose-5-phosphate aldolase, 2-deoxy-d-ribose-5-phosphate aldolase, deoxyribose-5-phosphate aldolase, deoxyribose-phosphate aldolase, deoxyribose 5-phosphate aldolase, 2-deoxy-d-ribose 5-phosphate aldolase, d5rp aldolase, 2-deoxyribose 5-phosphate aldolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Deoxyribose-5-phosphate aldolase
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-
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aldolase, deoxyribo
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-
-
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CGI-26
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Deoxyriboaldolase
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-
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Deoxyribose-5-phosphate aldolase
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DERA
DR aldolase
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-
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Phosphodeoxyriboaldolase
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DERA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
Schiff base intermediate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aldol condensation
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SYSTEMATIC NAME
IUBMB Comments
2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9026-97-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
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
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-
?
D-glyceraldehyde 3-phosphate + acetaldehyde
2-deoxy-D-ribose 5-phosphate
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-
-
r
(R)-3-Bromo-2-hydroxypropanal + acetaldehyde
5-Bromo-2-deoxyribose
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-
-
?
(S)-4-chloro-3-hydroxybutanal + acetaldehyde
(3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside
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-
-
-
?
2-hydroxy-3-butenal + acetaldehyde
2,5,6-trideoxy-D-erythro-5-hexenose
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-
-
?
3-azidopropanal + 2 acetaldehyde
(4R,6R)-6-(2-azidoethyl)-4-hydroxyoxan-2-one + 2 H+
-
-
-
?
3-azidopropionaldehyde + acetaldehyde
(4R,6R)-4-hydroxy-6-(2-triaz-2-en-1-ylethyl)tetrahydro-2H-pyran-2-one
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no activity with wild-type enzyme, mutant enzyme S238D gives 35% yield of the sequential aldol condensation product
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-
?
3-Chloro-2-hydroxypropanal + propionaldehyde
5-Chloro-2-methylribose
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-
-
?
3-chloropropionaldehyde + acetaldehyde
(4R,6S)-6-(2-chloroethyl)-4-hydroxytetrahydro-2H-pyran-2-one
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wild type enzyme gives 25% yield of the sequential aldol condensation product, mutant enzyme S238D gives 43% yield of the sequential aldol condensation product
-
-
?
3-Thioglyceraldehyde + acetaldehyde
2-Deoxy-5-thio-D-erythro-pentose
-
-
-
?
5-O-(4'-methylumbelliferyl)-2-deoxy-D-ribose
3-O-(4'-methylumbelliferyl)-D-glyceraldehyde + acetaldehyde
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-
-
-
?
D-(R)-3-Azido-2-hydroxypropanal + acetaldehyde
5-Azido-(2R)-methyl-2,5-dideoxy-D-ribo-furanose
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-
-
?
D-(R)-3-Azido-2-hydroxypropanal + acetone
6-Azido-1,3,5-trideoxy-D-erythro-hexulose
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-
-
?
D-(R)-3-Azido-2-hydroxypropanal + fluoroacetone
6-Azido-1-fluoro-1,3,5-trideoxy-D-erythro-hexulose
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-
-
?
D-2-deoxyribose
glyceraldehyde + acetaldehyde
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good substrate for the S238D mutant, weak substrate for the wild-type enzyme
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?
D-glyceraldehyde 3-phosphate + acetaldehyde
2-deoxy-D-ribose 5-phosphate
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-
-
-
?
D-Glyceraldehyde 3-phosphate + acetaldehyde
?
-
biosynthesis of deoxyribose 5-phosphate
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-
?
D-glyceraldehyde 3-phosphate + propionaldehyde
2-methyl-2-deoxypentose phosphate
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-
-
-
?
Isobutyraldehyde + fluoroacetone
(S)-1-Fluoro-3-hydroxy-4-methylhexan-2-one
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-
-
?
L-Glyceraldehyde 3-phosphate + acetaldehyde
Glyceraldehyde + acetaldehyde
-
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
r
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
-
-
-
-
?
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
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-
-
r
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
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-
-
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r
additional information
?
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sequential two-substrate and three-substrate aldol reactions
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-
?
additional information
?
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a new stereogenic center with 3(S) configuration is formed when acetaldehyde, fluoroacetone, or acetone. With propanal, two stereogenic centers are formed with 2(R) and 3(S) configuration
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-
?
additional information
?
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no activity with 3-nitropropionaldehyde + acetaldehyde, wild-type enzyme and mutant enzyme S238D
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
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-
-
r
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
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-
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r
D-Glyceraldehyde 3-phosphate + acetaldehyde
?
-
biosynthesis of deoxyribose 5-phosphate
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chloroacetaldehyde
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the enzyme is rapidly and irreversibly inactivated and loses 84.9% of its enzymatic activity in the presence of 200 mM chloroacetaldehyde
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
9.6
2-deoxy-D-ribose 5-phosphate
pH 8.0, 30°C, mutant enzyme S238I/S239I
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
2-deoxy-D-ribose 5-phosphate
pH 8.0, 30°C, mutant enzyme S238I/S239I
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
2-deoxy-D-ribose 5-phosphate
pH 8.0, 30°C, mutant enzyme S238I/S239I
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8
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cleavage of 2-deoxy-D-ribose 5-phosphate, enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
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pH 6.0: about 50% of maximal activity, pH 10.5: about 40% of maximal activity, soluble enzyme
6 - 11.5
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
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30°C: about 50% of maximal activity, 70°C: about 40% of maximal activity, soluble enzyme
30 - 85
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30°C: about 55% of maximal activity, 85°C: about 50% of maximal activity, enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilane nano-magnet material
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme immobilized on glutaraldehyde-(3-aminopropyl)triethoxysilanenano-magnet material exhibits a wider range of reaction temperatures than the free enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27200
27737
33000
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monomeric form, gel filtration in 10 mM Tris/HCl containing 50 mM KCl and 2 mM EDTA
50000
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dimeric form, gel filtration in 50 mM potassium phosphate buffer, pH 7.5
27737
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1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
27737
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2 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
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2 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
monomer
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1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of native wild-type enzyme and SeMet enzyme are grown by vapor-diffusion sitting drop method, analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S238P
completely abolished catalytic activity in the retro-aldol reaction
S238P/S239P
completely abolished catalytic activity in the retro-aldol reaction
S239P
the mutant enzyme increases the enthalpy change at the transition state, relative to the wild-type enzyme, but concomitant loss in entropy causes an overall relative loss in the TS free energy change. This entropy loss, as measured by the temperature dependence of catalysed rates, is mirrored in both a drastic loss in dynamics of the enzyme, which contributes to phosphate binding, as well as an overall loss in anti-correlated motions distributed over the entire protein
D84G/DELTAY259
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the catalytic activity towards 2-deoxy-D-ribose-5-phosphate cleavage is increased 4fold compared to the wild type enzyme
F200I
-
shows a nearly 14fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
K13C
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shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
M185T
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
M185V
-
mutation results in an about 5fold increase in (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation compared to the wild type enzyme
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
S238D
S239C
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
S93G/A174V
-
shows a nearly 3fold increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
T19I/I166T
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
T19S
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
S238D
-
mutant enzyme shows great improvement in catalytic activity towards sequential aldol reactions, mutant enzyme has wider specificity than wild-type enzyme, mutant enzyme shows activity with 3-azidopropionaldehyde and acetaldehyde, wild-type enzyme shows no activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 11.5
-
immobilized enzyme loses very little activity at pH values ranging from 5.5 to 11.5
748402
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme is an interesting candidate for bio-catalysis of carbo-ligation reactions, which are central to synthetic chemistry
industry
-
ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. 2-Deoxy-D-ribose-5-phosphate aldolase can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided
synthesis
synthesis
-
stereocontrolled aldol condensation of 3-hydroxy aldehydes and ketones
synthesis
-
synthesis of a variety of sugar analogs, including 2-deoxy-L-fucose and analogs, thiosugars and glycolipid precursors. The sequential aldol reaction is utilized in the synthesis of a variety of 2,4-dideoxyhexoses and 2,4,6-trideoxyhexoses
synthesis
-
mutant D-2-deoxyribose-5-phosphate aldolase Ser238Asp is used to prepare beta-hydroxy-delta lactol synthons and tert-butyl [(4R,6R)-6-aminoethyl-2,2-dimethyl-1,3-dioxn-4-yl]acetate, a key intermediate for atorvastatin synthesis
synthesis
-
industrial application of the enzyme for the synthesis of a key building block for the pharmaceutical blockbuster atorvastatin. The main drawback of the enzyme being used in such a process is its sensitivity to industrially relevant concentrations of the substrate and the occurrence of product inhibition. Product inhibition can be avoided by coupling the catalytic transformation with transport processes, which, in turn, would require an immobilization of the enzyme within a thin film that can be deposited on a membrane support. A fabrication process for such films is developed that is based on the formation of DERA-poly(N-isopropylacrylamide) conjugates that are subsequently allowed to self-assemble at an air-water interface to yield the respective film
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valentin-Hansen, P.; Boetius, F.; Hammer-Jespersen, K.; Svendsen, I.
The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase
Eur. J. Biochem.
125
561-566
1982
Escherichia coli
Racker, E.
Enzymatic synthesis and breakdown of desoxyribose phosphate
J. Biol. Chem.
196
347-365
1951
Escherichia coli, Escherichia coli 4157
Hespell, R.B.; Odelson, D.A.
Metabolism of RNA-ribose by Bdellovibrio bacteriovorus during intraperiplasmic growth on Escherichia coli
J. Bacteriol.
136
936-946
1978
Bdellovibrio bacteriovorus, Bdellovibrio bacteriovorus 109J, Escherichia coli
Stura, E.A.; Ghosh, S.; Garcia-Junceda, E.; Chen, L.; Wong, C.H.; Wilson, I.A.
Crystallization and preliminary crystallographic data for class I deoxyribose-5-phosphate aldolase from Escherichia coli: an application of reverse screening
Proteins Struct. Funct. Genet.
22
67-72
1995
Escherichia coli
Barbas, C.F.; Wang, Y.F.; Wong, C.H.
Deoxyribose-5-phosphate aldolase as a synthetic catalyst
J. Am. Chem. Soc.
112
2013-2014
1990
Escherichia coli
-
Chen, L.; Dumas, D.P.; Wong, C.H.
Deoxyribose-5-phosphate aldolase as a catalyst in asymetric aldol condensation
J. Am. Chem. Soc.
114
741-748
1992
Escherichia coli
-
Wong, C.H.; Garcia-Junceda, E.; Chen, L.; Blanco, O.; Gijsen, H.J.M.; Steensma, D.H.
Recombinant 2-deoxyribose-5-phosphate aldolase in organic synthesis: use of sequential two-substrate and three-substrate aldol reactions
J. Am. Chem. Soc.
117
3333-3339
1995
Escherichia coli, Escherichia coli DH5-alpha
-
DeSantis, G.; Liu, J.; Clark, D.P.; Heine, A.; Wilson, I.A.; Wong, C.H.
Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase
Bioorg. Med. Chem.
11
43-52
2003
Escherichia coli
Heine, A.; Luz, J.G.; Wong, C.H.; Wilson, I.A.
Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution
J. Mol. Biol.
343
1019-1034
2004
Escherichia coli (P0A6L0)
Liu, J.; Hsu, C.C.; Wong, C.H.
Sequential aldol condensation catalyzed by DERA mutant Ser238Asp and a formal total synthesis of atorvastatin
Tetrahedron Lett.
45
2439-2441
2004
Escherichia coli
-
Horinouchi, N.; Ogawa, J.; Kawano, T.; Sakai, T.; Saito, K.; Matsumoto, S.; Sasaki, M.; Mikami, Y.; Shimizu, S.
Efficient production of 2-deoxyribose 5-phosphate from glucose and acetaldehyde by coupling of the alcoholic fermentation system of Bakers yeast and deoxyriboaldolase-expressing Escherichia coli
Biosci. Biotechnol. Biochem.
70
1371-1378
2006
Escherichia coli, Escherichia coli 10B5/pTS8
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
Biotechnol. J.
1
537-548
2006
Escherichia coli
Horinouchi, N.; Ogawa, J.; Kawano, T.; Sakai, T.; Saito, K.; Matsumoto, S.; Sasaki, M.; Mikami, Y.; Shimizu, S.
One-pot microbial synthesis of 2-deoxyribonucleoside from glucose, acetaldehyde, and a nucleobase
Biotechnol. Lett.
28
877-881
2006
Escherichia coli, Escherichia coli 10B5/pTS8
Feron, G.; Mauvais, G.; Martin, F.; Semon, E.; Blin-Perrin, C.
Microbial production of 4-hydroxybenzylidene acetone, the direct precursor of raspberry ketone
Lett. Appl. Microbiol.
45
29-35
2007
Bacillus cereus, Bacillus subtilis, Escherichia coli
Stanton, C.L.; Houk, K.N.
Benchmarking pKa prediction methods for residues in proteins
J. Chem. Theory Comput.
4
951-966
2008
Escherichia coli (P0A6L0)
Reinicke, S.; Rees, H.C.; Espeel, P.; Vanparijs, N.; Bisterfeld, C.; Dick, M.; Rosencrantz, R.R.; Brezesinski, G.; de Geest, B.G.; Du Prez, F.E.; Pietruszka, J.; Boeker, A.
Immobilization of 2-deoxy-D-ribose-5-phosphate aldolase in polymeric thin films via the Langmuir-Schaefer Technique
ACS Appl. Mater. Interfaces
9
8317-8326
2017
Escherichia coli
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
ACS Catal.
4
3059-3068
2014
Escherichia coli (P0A6L0)
-
Zhang, S.; Bisterfeld, C.; Bramski, J.; Vanparijs, N.; De Geest, B.G.; Pietruszka, J.; Boeker, A.; Reinicke, S.
Biocatalytically active thin films via self-assembly of 2-deoxy-D-ribose-5-phosphate aldolase-poly(N-isopropylacrylamide) conjugates
Bioconjug. Chem.
29
104-116
2018
Escherichia coli
Ma, H.; Szeler, K.; Kamerlin, S.C.L.; Widersten, M.
Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)
Chem. Sci.
7
1415-1421
2016
Escherichia coli (P0A6L0)
Fei, H.; Xu, G.; Wu, J.; Yang, L.
Improvement of the thermal stability and aldehyde tolerance of deoxyriboaldolase via immobilization on nano-magnet material
J. Mol. Catal. B
101
87-91
2014
Escherichia coli
-
Bisterfeld, C.; Kberl, I.; Dick, M.; Pietruszka, J.
A fluorogenic screening for enantio- and diastereoselectivity of 2-deoxy-D-ribose-5-phosphate aldolases
Synlett
27
11-16
2016
Escherichia coli, Pyrobaculum aerophilum, Rhodococcus erythropolis, Thermotoga maritima, Colwellia psychrerythraea, Shewanella halifaxensis
-
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