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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-arabitol dehydrogenase, arabitol dehydrogenase, d-xylulose-forming d-arabitol dehydrogenase, aardh, nad-dependent d-arabitol dehydrogenase, d-arabinitol 4-dehydrogenase,
more
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D-xylulose-forming D-arabitol dehydrogenase
-
dehydrogenase, D-arabinitol
-
-
-
-
NAD-dependent D-arabitol dehydrogenase
-
arabitol dehydrogenase
-
-
-
-
arabitol dehydrogenase
-
-
D-arabitol dehydrogenase
-
-
-
-
D-arabitol dehydrogenase
-
-
D-arabitol dehydrogenase
-
-
-
D-arabitol dehydrogenase
-
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D-arabinitol + NAD+ = D-xylulose + NADH + H+
-
-
-
-
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D-arabinitol:NAD+ 4-oxidoreductase
-
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D-arabinitol + NAD+
D-ribulose + NADH + H+
D-arabinitol + NAD+
D-xylulose + NADH + H+
D-arabitol + NAD+
D-xylulose + NADH + H+
D-arabitol + NADP+
D-xylulose + NADPH + H+
-
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
-
-
-
?
D-glucitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
D-ribulose + NADH + H+
D-arabinitol + NAD+
-
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
sorbose + NADH + H+
10.3% activity with D-sorbitol compared to D-arabitol
-
-
r
D-xylulose + NADH + H+
D-arabitol + NAD+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
glycerol + NAD+
dihydroxyacetone + NADH + H+
L-Xylulose + NADH
?
-
3% activity
-
-
?
meso-erythritol + NAD+
? + NADH + H+
-
-
-
?
meso-erythritol + NAD+
L-erythrose + NADH + H+
5.3% activity with D-sorbitol compared to D-arabitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
additional information
?
-
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
recombinant protein from Saccharomyces cerevisiae
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
D-arabitol i.e. D-arabinitol
-
?
D-arabitol + NAD+
D-xylulose + NADH + H+
is the optimal substrate for aArDH
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-
r
D-arabitol + NAD+
D-xylulose + NADH + H+
best substrates in both reaction directions
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
30.5% and 54.8% activity with D-mannitol and D-fructose compared to D-arabitol and D-xylulose, respectively
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
1.9% activity with D-sorbitol compared to D-arabitol
-
-
?
Galactitol + NAD+
?
-
-
-
-
?
Galactitol + NAD+
?
-
1.6% activity
-
-
?
Galactitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
-
-
-
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
6.2% activity with D-sorbitol compared to D-arabitol
-
-
?
Xylitol + NAD+
?
-
-
-
-
?
Xylitol + NAD+
?
-
5% activity
-
-
?
Xylitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
8.8% activity with D-sorbitol compared to D-arabitol
-
-
r
additional information
?
-
-
no activity with D-mannitol
-
-
?
additional information
?
-
-
both purified native and recombinant aArDH do not accept L-arabitol as substrate
-
-
?
additional information
?
-
both purified native and recombinant aArDH do not accept L-arabitol as substrate
-
-
?
additional information
?
-
-
no substrate: L-arabinitol
-
-
?
additional information
?
-
no substrate: L-arabinitol
-
-
?
additional information
?
-
-
D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
-
-
?
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D-arabinitol + NAD+
D-ribulose + NADH + H+
D-arabinitol + NAD+
D-xylulose + NADH + H+
D-ribulose + NADH + H+
D-arabinitol + NAD+
-
-
-
-
?
additional information
?
-
-
D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
recombinant protein from Saccharomyces cerevisiae
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
D-arabitol i.e. D-arabinitol
-
?
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NAD+
-
-
NAD+
NAD+ is preferred over NADP+
NAD+
aArDH prefers NAD+ to NADP+ as coenzyme
NAD+
the enzyme harbors the NAD(P)-binding motif TGXXXGXG, preferred substrate
NADH
-
-
NADP+
-
NADP+
NAD+ is preferred over NADP+
additional information
-
no activity with NADPH
-
additional information
-
no activity with NADPH
-
additional information
-
no activity with NADPH
-
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Ba2+
up to 200 mM, 2fold increase in activity
Ca2+
up to 200 mM, 2fold increase in activity
Mg2+
-
1-5 mM increases activity about 50%, also enhances stability
additional information
-
not stimulatory: Mn2+, Ni2+, Mg2+
additional information
not stimulatory: Mn2+, Ni2+, Mg2+
additional information
-
no divalent cations are required for activity
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1,10-phenanthroline
-
2 mM, 37% inhibition
2,2'-dipyridyl
-
2 mM, 19% inhibition
Cu2+
10 mM, complete inhibition. Activity can partly be restored by addition of EDTA
CuSO4
inactivates aArDH activity, which is restored by 80% by addition of 100 mM EDTA at pH 8.0
diethyldithiocarbamate
-
10 mM, 28% inhibition
Zn2+
up to 200 mM, slight inhibition
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3.5
D-arabinitol
-
-
4.5
D-arabinitol
pH 8.5, 25°C
3.8
D-arabitol
pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+
6.1
D-mannitol
-
-
78.5
D-mannitol
pH 8.5, 25°C
127.3
D-sorbitol
-
127.3
D-sorbitol
pH 8.5, 25°C
1.14
D-xylulose
-
-
28.1
D-xylulose
pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH
133.6
glycerol
-
133.6
glycerol
pH 8.5, 25°C
0.04
NAD+
-
-
0.05
NAD+
pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+
0.036
NADH
-
-
0.21
NADH
pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH
242.8
ribitol
-
242.8
ribitol
pH 8.5, 25°C
18.5
xylitol
-
177.2
xylitol
pH 8.5, 25°C
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876
D-arabinitol
pH 8.5, 25°C
35.3
D-mannitol
-
35.3
D-mannitol
pH 8.5, 25°C
19.7
D-sorbitol
-
19.7
D-sorbitol
pH 8.5, 25°C
16.3
glycerol
-
16.3
glycerol
pH 8.5, 25°C
13.4
ribitol
-
13.4
ribitol
pH 8.5, 25°C
177.2
xylitol
-
177.2
xylitol
pH 8.5, 25°C
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194.7
D-arabinitol
pH 8.5, 25°C
0.45
D-mannitol
pH 8.5, 25°C
0.15
D-sorbitol
pH 8.5, 25°C
0.12
glycerol
pH 8.5, 25°C
0.06
ribitol
pH 8.5, 25°C
9.58
xylitol
pH 8.5, 25°C
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0.17
-
lysates of Escherichia coli, transformed with enzyme gene
0.2
-
D-xylulose, of recombinant protein
0.37
-
lysates of Saccharomyces cerevisiae, transformed with enzyme gene
0.55
recombinant aArDH with meso-erythritol as substrate
0.87
recombinant aArDH with ethanol as substrate
1.5
recombinant aArDH with ribitol as substrate
1.7
pH 8.5, 30°C, substrates ethanol and NAD+, recombinant His-tagged enzyme
16.4
recombinant aArDH with D-xylulose as substrate
16.66
119fold purified enzyme
187
-
of recombinant protein
2.1
recombinant aArDH with glycerol as substrate
2.5
recombinant aArDH with D-fructose as substrate
2.8
recombinant aArDH with D-sorbitol as substrate
22.9
pH 5.5, 30°C, substrates D-xylulose and NADH, recombinant His-tagged enzyme
26.8
pH 8.5, 30°C, substrates D-mannitol and NAD+, recombinant His-tagged enzyme
4.2
recombinant aArDH with D-mannitol as substrate
4.7
pH 8.5, 30°C, substrates meso-erythritol and NAD+, recombinant His-tagged enzyme
5.5
pH 8.5, 30°C, substrates glycerol and NAD+, recombinant His-tagged enzyme
68.25
-
D-arabinitol, of recombinant protein
7.7
pH 8.5, 30°C, substrates xylitol and NAD+, recombinant His-tagged enzyme
87.7
pH 8.5, 30°C, substrates D-arabitol and NAD+, recombinant His-tagged enzyme
9
pH 8.5, 30°C, substrates D-sorbitol and NAD+, recombinant His-tagged enzyme
additional information
-
grown on medium with D-arabinitol, specific activity of crude cell extract: 1.13-3.47
12.6
recombinant aArDH with xylitol as substrate
12.6
pH 5.5, 30°C, substrates D-fructose and NADH, recombinant His-tagged enzyme
68.5
pH 8.5, 25°C
68.5
recombinant aArDH with 100 mM D-arabitol as substrate
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6.5
-
optimal activity, reduction
9
-
D-arabinitol, D-mannitol
5.5
optimum for ketone reduction
5.5
reduction of D-xylulose with NADH, recombinant His-tagged enzyme
8.5
optimum pH for oxidation is 8.5, with 0.7% and 5.6% of the maximum activity at pH 5.0 and 14, respectively. Optimal pH for reduction is 5.5, with 2 and 10% of the maximum activity at pH 4.5 and 8.0
8.5
optimum for polyol oxidation
8.5
oxidation of D-arabitol with NAD+, recombinant His-tagged enzyme
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10 - 11
-
enzyme activity increases with increasing pH, measurements above pH 11.0 not feasible
3 - 7
reduction of D-xylulose with NADH, over 80% of maximal activity within this range, recombinant His-tagged enzyme
6 - 11
oxidation of D-arabitol with NAD+, over 60% of maximal activity within this range, recombinant His-tagged enzyme
6 - 8.5
-
pH 6.0: about 60% of maximum activity, pH 8.5: about 60% of activity maximum
7.5 - 10
-
at pH 7.5 and 10.0 about 50% relative activity, D-arabinitol
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30
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
30
both reaction directions, recombinant His-tagged enzyme
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25 - 55
oxidation and reduction activities of ArDH, over 80% of maximal activity at 24-40°C, and below 60% of maximal activity when the temperature exceeds 55°C, recombinant His-tagged enzyme
30 - 50
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
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5.88
isoelectric focusing
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and strains WO-1, 1006, 1001
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-
brenda
and strains WO-1, 1006, 1001
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-
brenda
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-
brenda
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-
brenda
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-
brenda
isolated from a sample of vinegar residue
UniProt
brenda
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-
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brenda
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-
-
brenda
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-
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brenda
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-
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brenda
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UniProt
brenda
-
-
-
brenda
i.e. Klebsiella pneumoniae, gene expression in Escherichia coli K12
-
-
brenda
strain P14 (guanine auxotroph), derived from strain 1033
-
-
brenda
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evolution
enzyme ArDH containing a NAD(P)-binding motif TGXXX[AG]XG and a classical active site motif belongs to the short-chain dehydrogenase family
additional information
ArDH has a conserved sequence region of TGXXXGXG, in this NAD(P)-binding motif, glycine-rich region plays a critical role in the stability of this kind of domain. Conserved domain of YXXXK, a classical active site motif, accompanying with two conserved amino acids N119 and S147 in the upstream, is also found in ArDH, sequence comparisons. Structure-function analysis of ArDH, and structure homology modeling using the structure of putative polyol dehydrogenase (PDB ID 3AWD) from Gluconobacter oxydans strain DSM2343 as template, overview
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110000
-
native gradient PAGE
28000
4 * 28500, calculated, 4 * 28000, SDS-PAGE
30000
-
4 * 30000, calculated from gene sequence and molecular weight of native enzyme
30643
-
x * 30643, calculated from gene sequence
30748
-
x * 30748, gene sequence
31000
-
x * 31000, SDS-PAGE
43000
-
gel filtration, ultracentrifugation
44000
-
sedimentation equilibrium
46000
-
calculated from amino acid composition
46500
-
1 * 46500, SDS-PAGE
28500
native aArDH, 2 * 28500, SDS-PAGE
28500
recombinant aArDH, 2 * 28500, SDS-PAGE
28500
4 * 28500, calculated, 4 * 28000, SDS-PAGE
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heterodimer
native aArDH, 2 * 28500, SDS-PAGE
homodimer
recombinant aArDH, 2 * 28500, SDS-PAGE
monomer
-
1 * 46500, SDS-PAGE
?
-
x * 30643, calculated from gene sequence
?
-
x * 30643, calculated from gene sequence
-
?
-
x * 30748, gene sequence
tetramer
4 * 28500, calculated, 4 * 28000, SDS-PAGE
tetramer
-
4 * 30000, calculated from gene sequence and molecular weight of native enzyme
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additional information
in the co-biotransformation by the whole cells of recombinant Escherichia coli BL21(DE3)-ardh and BL21(DE3)-xdh strains, 26.1 g/l xylitol is produced from 30 g/l D-arabitol in 22 h with a yield 0.87 g/g. The xylitol production is increased by more than two times as compared with that of Gluconobacter sp. alone, and is improved 10.1% than that of Gluconobacter sp. mixed with Escherichia coli strain BL21(DE3)-xdh
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6 - 9.5
-
more labile at increasing pH from 6.0-9.5
9566
8.5 - 12
very stable in alkaline buffer
701082
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45
-
half-life: 7 min
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-15°C, after ammonium sulfate fractionation, pH 7.0, stable for at least one year without loss in activity, higher activity with potassium phosphate buffer than with glycine-HCl
-
-20°C, protein concentration 50 mg/ml, 50% v/v glycerol, stable 3 months, loss of activity less than 50%
-
4°C, 100 mM Tris/HCl buffer, 2 mM 2-mercaptoethanol, 50 days
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol for 50 days, 50% loss of activity. Addition of 2-mercaptoethanol is required
frozen after second calcium phosphate gel preparation, stable for 3 years
-
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recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant protein from Escherichia coli
-
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expression in Escherichia coli
expression vector containing the ORF of aArDH under the control of T7 promoter, pET21aArDH, transformed into Escherichia coli strain BL21(DE3)
gene ardh, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene over-expressed in Escherichia coli BW31M
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gene over-expressed in Escherichia coli K12
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gene over-expressed in S. cerevisiae BWG 1-7A and in Escherichia coli JM109, DH5-alpha
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gene over-expressed in Saccharomyces cerevisiae S700
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Oryza sativa is transformed with a plant-expression-optimized synthetic gene using Biolistic-mediated transformation. The atlD gene is integrated into the rice genome of selected plants and is inherited in a Mendelian manner
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recombinant expression of the yeast enzyme in Nicotiana tabacum using the chloroplast transformation vector pMSK83 harboring aadA and ArDH genes under the control of chloroplast regulatory sequences
-
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ArDH enzyme expression in tobacco chloroplasts confers tolerance to NaCl (up to 400 mM). Transgenic plants compared to wild-type survived for only 4-5 weeks on 400 mM NaCl whereas plants remain green and grow normal on concentrations up to 350 mM NaCl. A-week-old seedlings are also challenged with PEG up to 6% in the liquid medium, considering that membranes and proteins are protected under stress conditions due to accumulation of arabitol in chloroplasts. Seedlings are tolerant to 6% PEG, suggesting that ARDH enzyme maintains integrity of membranes in chloroplasts under drought conditions via metabolic engineering
-
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agriculture
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the gene can be expressed in agronomic plants to withstand abiotic stresses
biotechnology
-
the gene can be expressed in agronomic plants to withstand abiotic stresses
industry
promising method for the production of xylitol from the cheap material glucose if the aArDH gene can be introduced into yeast strains that can convert glucose to D-arabitol
analysis
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potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker
analysis
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potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker
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Wong, B.; Murray, J.S.; Castellanos, M.; Croen, K.D.
D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase
J. Bacteriol.
175
6314-6320
1993
Candida albicans, Candida albicans B331
brenda
Quong, M.W.; Miyada, C.G.; Switchenko, A.C.; Goodman, T.C.
Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis
Biochem. Biophys. Res. Commun.
196
1323-1329
1993
Candida tropicalis
brenda
Neuberger, M.S.; Patterson, R.A.; Hartley, B.S.
Purification and properties of Klebsiella aerogenes D-arabitol dehydrogenase
Biochem. J.
183
31-42
1979
Klebsiella aerogenes
brenda
Wilson, B.L.; Mortlock, R.P.
Regulation of D-xylose and D-arabitol catabolism by Aerobacter aerogenes
J. Bacteriol.
113
1404-1411
1973
Klebsiella aerogenes, Klebsiella aerogenes PRL-R3
brenda
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