Information on EC 4.1.2.4 - deoxyribose-phosphate aldolase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.2.4
-
RECOMMENDED NAME
GeneOntology No.
deoxyribose-phosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2'-deoxy-alpha-D-ribose 1-phosphate degradation
-
-
Pentose phosphate pathway
-
-
purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-97-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K1
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
UKi2
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 10B5/pTS8
-
-
Manually annotated by BRENDA team
4157
-
-
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
lamb and adult
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
JN665070
GenBank
Manually annotated by BRENDA team
-
JN665070
GenBank
Manually annotated by BRENDA team
strain GS-5
SwissProt
Manually annotated by BRENDA team
strain GS-5
SwissProt
Manually annotated by BRENDA team
strain ATCC BAA-854 (0140J)
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
HB8
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-3-Bromo-2-hydroxypropanal + acetaldehyde
5-Bromo-2-deoxyribose
show the reaction diagram
(S)-4-chloro-3-hydroxybutanal + acetaldehyde
(3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside
show the reaction diagram
2-deoxy-D-ribose
D-glyceraldehyde + acetaldehyde
show the reaction diagram
2-deoxy-D-ribose 5-phosphate
?
show the reaction diagram
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
show the reaction diagram
2-deoxy-D-ribose-5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
show the reaction diagram
-
-
-
?
2-hydroxy-3-butenal + acetaldehyde
2,5,6-trideoxy-D-erythro-5-hexenose
show the reaction diagram
3-Azido-3-deoxy-erythrose + acetaldehyde
5-Azidohexofuranose
show the reaction diagram
-
-
-
-
3-azidopropinaldehyde + acetaldehyde
deoxy-azidoethyl pyranose + ?
show the reaction diagram
-
-
-
?
3-azidopropionaldehyde + acetaldehyde
(4R,6R)-4-hydroxy-6-(2-triaz-2-en-1-ylethyl)tetrahydro-2H-pyran-2-one
show the reaction diagram
-
no activity with wild-type enzyme, mutant enzyme S238D gives 35% yield of the sequential aldol condensation product
-
-
?
3-Chloro-2-hydroxypropanal + propionaldehyde
5-Chloro-2-methylribose
show the reaction diagram
3-chloropropionaldehyde + acetaldehyde
(4R,6S)-6-(2-chloroethyl)-4-hydroxytetrahydro-2H-pyran-2-one
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
chloroacetaldehyde + acetaldehyde
(S)-4-chloro-3-hydroxybutanal
show the reaction diagram
D-(R)-3-Azido-2-hydroxypropanal + acetaldehyde
5-Azido-(2R)-methyl-2,5-dideoxy-D-ribo-furanose
show the reaction diagram
-
-
-
-
D-(R)-3-Azido-2-hydroxypropanal + acetone
6-Azido-1,3,5-trideoxy-D-erythro-hexulose
show the reaction diagram
-
-
-
-
D-(R)-3-Azido-2-hydroxypropanal + fluoroacetone
6-Azido-1-fluoro-1,3,5-trideoxy-D-erythro-hexulose
show the reaction diagram
-
-
-
-
D-2-deoxyribose
glyceraldehyde + acetaldehyde
show the reaction diagram
-
good substrate for the S238D mutant, weak substrate for the wild-type enzyme
-
?
D-Erythrose + acetaldehyde
2,3,4,5-Trihydroxypentanal
show the reaction diagram
-
-
-
-
-
D-Erythrose 4-phosphate + acetaldehyde
?
show the reaction diagram
-
-
-
-
-
D-Glyceraldehyde 3-phosphate + acetaldehyde
2-Deoxy-D-ribose 5-phosphate
show the reaction diagram
D-Glyceraldehyde 3-phosphate + acetaldehyde
?
show the reaction diagram
D-Glyceraldehyde 3-phosphate + propionaldehyde
2-Methyl-2-deoxypentose phosphate
show the reaction diagram
D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
-
Glyceraldehyde phosphate + acetaldehyde
Hydroxyacetaldehyde + glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
Isobutyraldehyde + acetone
(S)-4-Hydroxy-5-methylhexan-2-one
show the reaction diagram
-
-
-
-
Isobutyraldehyde + fluoroacetone
(S)-1-Fluoro-3-hydroxy-4-methylhexan-2-one
show the reaction diagram
-
-
-
-
L-Glyceraldehyde 3-phosphate + acetaldehyde
Glyceraldehyde + acetaldehyde
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-ribose 5-phosphate
?
show the reaction diagram
2-deoxy-D-ribose 5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
show the reaction diagram
D-Glyceraldehyde 3-phosphate + acetaldehyde
?
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetaldehyde
acrolein
-
irreversible, no inactivation after prolonged incubation with glycidol phosphate and glycidaldehyde
Chloral hydrate
-
-
Chloroacetaldehyde
-
the enzyme is rapidly and irreversibly inactivated and loses 84.9% of its enzymatic activity in the presence of 200 mM chloroacetaldehyde
hydroxylamine
-
-
Octanol
-
-
p-hydroxymercuribenzoate
-
2-mercaptoethanol or dithiothreitol prevent inactivation
propionaldehyde
-
-
Zn2+
1 mM, 35% decrease in activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
activates
acetaldehyde
the enzyme shows the highest activity at up to 100 mM acetaldehyde, and also shows some activity at 300 mM acetaldehyde
acetate
-
activates
adipate
-
activates
cis-aconitate
-
activates
citrate
DL-isocitrate
-
activates
fumarate
Fumarate monomethyl ester
-
activates
Glutarate
Isobutanoate
-
activates
malate
Maleate
malonate
-
activates
propionate
-
activates
succinate
tricarballylate
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
418
2-deoxy-D-ribose
JN665070
pH 7.0, 25°C
0.02 - 145
2-deoxy-D-ribose 5-phosphate
9.1
2-deoxy-D-ribose-5-phosphate
in 100 mM Tris-HCl buffer, pH 8.8, 0.3 mM NADH, 10 U alcohol dehydrogenase, 1 mM 2-deoxy-D-ribose-5-phosphate
0.267 - 3.5
acetaldehyde
24 - 54.6
Chloroacetaldehyde
33 - 67
D-2-deoxyribose
0.2 - 0.71
D-glyceraldehyde 3-phosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.23
2-deoxy-D-ribose
Rhodococcus erythropolis
JN665070
pH 7.0, 25°C
0.58 - 521
2-deoxy-D-ribose 5-phosphate
0.022 - 0.21
D-2-deoxyribose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029
2-deoxy-D-ribose
Rhodococcus erythropolis
JN665070
pH 7.0, 25°C
2811
3.78
2-deoxy-D-ribose 5-phosphate
Rhodococcus erythropolis
JN665070
pH 7.0, 25°C
1173
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
acetaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
-
-
0.2
crude cell extract, in 100 mM sodium acetate buffer (pH 5.5) at 25°C
0.25
-
native enzyme, at 25°C
0.5
after 2.5fold purification, in 100 mM sodium acetate buffer (pH 5.5) at 25°C
1
-
native enzyme, at 25°C
44
crude extract, using 2-deoxy-D-ribose 5-phosphate as substrate, in 100 mM Tris-HCl buffer (pH 8.8), at 50°C
56
crude extract
58
-
recombinant enzyme, at 25°C
62
after 1.4fold purification, using 2-deoxy-D-ribose 5-phosphate as substrate, in 100 mM Tris-HCl buffer (pH 8.8), at 50°C
137
2.4fold purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
active in the range without exhibiting a sharp optimum
7.4 - 7.5
-
with deoxyribose 5-phospohate in either Tris or phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
more than 65% activity between pH 5.0 and 6.0, enzyme activity decreases sharply below pH 5.0 and above pH 7.0
6 - 7
-
pH 6: about 35% of maximal activity, pH 7: about 60% of maximal activity
6.5 - 7.5
at least 75% of maximum activity
9
JN665070
80% of maximum activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
JN665070
85% of maximum activity
70 - 80
the enzyme exhibits similar activity at temperatures between 70-80°C. The activity sharply decreases below 70°C and above 80°C
85 - 100
85°C: about 35% of maximal activity, 100°C: about 95% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.44
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
induced by growth on deoxyribonucleosides
Manually annotated by BRENDA team
-
Activity peaks in the late G2 phase, followed by a rapid decline during mitosis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aquifex aeolicus (strain VF5)
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Lactobacillus brevis (strain ATCC 367 / JCM 1170)
Mycobacterium avium (strain 104)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Shewanella halifaxensis (strain HAW-EB4)
Streptococcus suis (strain GZ1)
Streptococcus suis (strain GZ1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Toxoplasma gondii (strain ATCC 50861 / VEG)
Toxoplasma gondii (strain ATCC 50861 / VEG)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22900
JN665070
2 * 22900, calculated, 2 * 2000, SDS-PAGE
23300
calculated from amino acid sequence
24000
4 * 24000, SDS-PAGE
24800
x * 24800, SDS-PAGE
26000
2 * 26000, SDS-PAGE
26300
-
2 * 26300, SDS-PAGE
26400
2 * 26400, calculated from amino acid sequence
26600
2 * 26600, calculated and SDS-PAGE
27200
-
1 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE; 2 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE
27737
-
1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence; 2 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
31000
-
predicted; transfected HEK-293T cells, determined by SDS-PAGE and Western blot analysis
33000
-
monomeric form, gel filtration in 10 mM Tris/HCl containing 50 mM KCl and 2 mM EDTA
44000
JN665070
gel filtration
50000
-
dimeric form, gel filtration in 50 mM potassium phosphate buffer, pH 7.5
52000
gel filtration
53700
-
gel filtration
70000
-
gel filtration
93000
gel-filtration
253000
-
monomeric form, sucrose density gradient centrifugation
535000
-
dimeric form, sucrose density gradient centrifugation
700000
-
trimeric form, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 26000, SDS-PAGE; 2 * 26400, calculated from amino acid sequence
monomer
-
1 * 27200, the enzyme exists as monomer and as dimer, SDS-PAGE; 1 * 27737, enzyme exists as monomer and as dimer, calculation from DNA sequence
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
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
-
hanging drop vapour diffusion method with 20% (w/v) polyethylene glycol 1000, 0.2 M zinc acetate, and 0.1 M acetate buffer (pH 4.5)
-
microbatch method, crystal structure of the enzyme and its complex with 2-deoxy-D-ribose 5-phosphate
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
after heating at pH levels ranging from 4.0 to 11.0 for 30 min at 50°C, the enzyme shows no loss of activity
713699
5 - 11
5.5
-
the recombinant enzyme shows significant loss of activity at pH less than 5.5
677701
6.5 - 10.6
-
optimal stability in the range
5180
9
JN665070
half-life 20 days
728016
10
-
the recombinant enzyme shows significant loss of activity at pH above 10
677701
additional information
-
citrate stabilizes below pH 6.5
5180
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
30 min, no significant loss of activity
58
-
3 min, small loss of activity
60
the enzyme retains full activity after 1 h at 35-55°C, the enzyme retains 80% activity after incubation at 60°C for 1 h, almost no activity is observed after 1 h at 65°C
65
JN665070
half-life 2 min
70
-
rapid inactivation above
90 - 100
100
no loss of activity after 10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
citrate stabilizes below pH 6.5
-
not stable to freezing. Loses all activity when frozen and thawed
-
stabilization by 0.01 M MgCl2 or sulfhydryl reagents
-
the enzyme retains more than 75% activity after exposure for 8 h to 300 mM acetaldehyde at 25°C.
the enzyme shows stability toward a high concentration of acetaldehyde (100 mM)
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-dioxane
the enzyme retains 28% and 78% activity in 20% (v/v) and 5% (v/v) 1,4-dioxane, respectively
acetaldehyde
acetonitrile
the enzyme loses activity completely in 20% (v/v) and shows 64% activity in 5% (v/v) acetonitrile
dimethyl sulfoxide
Ethanol
Ethyl acetate
isopropanol
the enzyme retains 11% and 72% activity in 20% (v/v) and 5% (v/v) isopropanol, respectively
Methanol
methyl-tert-butylether
JN665070
20%, about 50-60% residual activity
N,N-dimethylformamide
stable up to 50% for 30 min at 50°C
tetrahydrofuran
the enzyme loses activity completely in 20% (v/v) and shows 72% activity in 5% (v/v) tetrahydrofuran
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for 1 year
-
4°C, in ammonium sulfate solution, stable
-
4°C, stable for 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by Ni-NTA affinity chromatography, 2.4fold, with a yield of 43%
large scale
-
Ni-NTA agarose column chromatography
recombinant protein
Superdex 200 gel filtration and DEAE-Toyopearl column chromatography
the GST-fused protein is affinity purified by glutathione-Sepharose beads
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) from pET303-DERA008 in both batch and fed-batch cultures, under the control of the IPTG-inducible T7 promoter
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expression in Escherichia coli
-
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expressed in Escherichia coli strain BL21 Star (DE3)
-
expressed in Escherichia coli strain BL21(DE3)
-
expressen in Escherichia coli
expression in Escherichia coli
into a pET302/NT-his expression vector and overexpressed in Escherichia coli BL21 (DE3)
into the vector pGEX-6P-2 for expression in Escherichia coli BL21DE3 pLysS cells and into pcDNA6/V5-HisA for transfection of HEK-293T cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2 mmol IPTG induces the expression of DERA. As the induction proceeds, the target protein expression level first increases and then decreases, and DERA concentration improves and reaches a plateau after 6 h of induction. DERA concentration increases with the biomass growth and peaks at the end of the culture period at 5.12 g/l with total volumetric productivity of 0.256 gl-1h-1, which are over 10 and 5fold higher than conventional batch culture, respectively
-
is induced by the fluoroquinolone antibiotic ciprofloxacin
-
lactose can induce DERA formation efficiently as isopropyl-beta-D-thiogalactoside. The enzyme concentration increases with the lactose content and reaches a plateau at a concentration of 2.0 g/l
-
when the concentration of acetate is over 1.0 g/l, DERA expression level decreases
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D84G/DELTAY259
-
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
G205E
-
decreased activity towards the natural substrate
K13C
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
K172E
-
decreased activity towards the natural substrate
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
R207E
-
altered substrate specificity
S239C
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
S239E
-
decreased activity towards the natural substrate
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
D84G/DELTAY259
-
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
-
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
-
T19S
-
shows a slight increase in productivity for (3R,5S)-6-chloro-2,4,6-trideoxyhexapyranoside formation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis
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