Information on EC 1.1.1.11 - D-arabinitol 4-dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
D-arabinitol 4-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NAD+ = D-xylulose + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-arabitol degradation
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degradation of sugar alcohols
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Pentose and glucuronate interconversions
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Fructose and mannose metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 4-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-18-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and strains WO-1, 1006, 1001
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Manually annotated by BRENDA team
and strains WO-1, 1006, 1001
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
D-arabinitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
D-arabitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Q308C1;
is the optimal substrate for aArDH
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-
r
D-fructose + NADH + H+
D-mannitol + NAD+
show the reaction diagram
Q308C1;
-
-
-
?
D-glucitol + NAD+
?
show the reaction diagram
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
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-
?
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-ribulose + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
-
-
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
D-xylulose + NADH + H+
D-arabitol + NAD+
show the reaction diagram
Q308C1;
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
Galactitol + NAD+
?
show the reaction diagram
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
L-Xylulose + NADH
?
show the reaction diagram
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3% activity
-
-
?
meso-erythritol + NAD+
? + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
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
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
D-arabinitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
D-ribulose + NADH + H+
D-arabinitol + NAD+
show the reaction diagram
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?
additional information
?
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
Q308C1;
; NAD+ is preferred over NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
Q308C1;
up to 200 mM, 2fold increase in activity
Ca2+
Q308C1;
up to 200 mM, 2fold increase in activity
Mg2+
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1-5 mM increases activity about 50%, also enhances stability
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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2 mM, 37% inhibition
2,2'-dipyridyl
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2 mM, 19% inhibition
Cu2+
Q308C1;
10 mM, complete inhibition. Activity can partly be restored by addition of EDTA
CuSO4
Q308C1;
inactivates aArDH activity, which is restored by 80% by addition of 100 mM EDTA at pH 8.0
diethyldithiocarbamate
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10 mM, 28% inhibition
Zn2+
Q308C1;
up to 200 mM, slight inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arabitol
Q308C1;
inducer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 39.8
D-arabinitol
4.5
D-arabitol
Q308C1;
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6.1 - 78.5
D-mannitol
127.3
D-sorbitol
Q308C1;
; pH 8.5, 25°C
1.14 - 2
D-xylulose
133.6
glycerol
Q308C1;
; pH 8.5, 25°C
0.04 - 0.2
NAD+
242.8
ribitol
Q308C1;
; pH 8.5, 25°C
18.5 - 177.2
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
876
D-arabinitol
Q308C1;
pH 8.5, 25°C
876
D-arabitol
Q308C1;
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35.3
D-mannitol
Q308C1;
; pH 8.5, 25°C
19.7
D-sorbitol
Q308C1;
; pH 8.5, 25°C
16.3
glycerol
Q308C1;
; pH 8.5, 25°C
13.4
ribitol
Q308C1;
; pH 8.5, 25°C
177.2
xylitol
Q308C1;
; pH 8.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
194.7
D-arabinitol
Q308C1;
pH 8.5, 25°C
0.45
D-mannitol
Q308C1;
pH 8.5, 25°C
0.15
D-sorbitol
Q308C1;
pH 8.5, 25°C
0.12
glycerol
Q308C1;
pH 8.5, 25°C
0.06
ribitol
Q308C1;
pH 8.5, 25°C
9.58
xylitol
Q308C1;
pH 8.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.14
Q308C1;
crude extract
0.17
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lysates of Escherichia coli, transformed with enzyme gene
0.2
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D-xylulose, of recombinant protein
0.37
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lysates of Saccharomyces cerevisiae, transformed with enzyme gene
0.55
Q308C1;
recombinant aArDH with meso-erythritol as substrate
0.87
Q308C1;
recombinant aArDH with ethanol as substrate
1.5
Q308C1;
recombinant aArDH with ribitol as substrate
2.1
Q308C1;
recombinant aArDH with glycerol as substrate
2.5
Q308C1;
recombinant aArDH with D-fructose as substrate
2.8
Q308C1;
recombinant aArDH with D-sorbitol as substrate
4.2
Q308C1;
recombinant aArDH with D-mannitol as substrate
12.6
Q308C1;
recombinant aArDH with xylitol as substrate
16.4
Q308C1;
recombinant aArDH with D-xylulose as substrate
16.66
Q308C1;
119fold purified enzyme
68.25
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D-arabinitol, of recombinant protein
68.5
Q308C1;
pH 8.5, 25°C; recombinant aArDH with 100 mM D-arabitol as substrate
187
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of recombinant protein
additional information
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grown on medium with D-arabinitol, specific activity of crude cell extract: 1.13-3.47
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
Q308C1;
optimum for ketone reduction
6.5
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optimal activity, reduction
8.5
Q308C1;
optimum for polyol oxidation; 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
9
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D-arabinitol, D-mannitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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pH 6.0: about 60% of maximum activity, pH 8.5: about 60% of activity maximum
7.5 - 10
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at pH 7.5 and 10.0 about 50% relative activity, D-arabinitol
10 - 11
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enzyme activity increases with increasing pH, measurements above pH 11.0 not feasible
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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enzyme assay at
28
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enzyme assay at
30
Q308C1;
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
Q308C1;
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.88
Q308C1;
isoelectric focusing
5.9
Q308C1;
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
Q308C1;
4 * 28500, calculated, 4 * 28000, SDS-PAGE
28500
Q308C1;
4 * 28500, calculated, 4 * 28000, SDS-PAGE; native aArDH, 2 * 28500, SDS-PAGE; recombinant aArDH, 2 * 28500, SDS-PAGE
30000
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4 * 30000, calculated from gene sequence and molecular weight of native enzyme
30643
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x * 30643, calculated from gene sequence
30748
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x * 30748, gene sequence
31000
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x * 31000, SDS-PAGE
43000
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gel filtration, ultracentrifugation
44000
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sedimentation equilibrium
46000
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calculated from amino acid composition
46500
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1 * 46500, SDS-PAGE
110000
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native gradient PAGE
140000
Q308C1;
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Q308C1;
native aArDH, 2 * 28500, SDS-PAGE
homodimer
Q308C1;
recombinant aArDH, 2 * 28500, SDS-PAGE
monomer
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1 * 46500, SDS-PAGE
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
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more labile at increasing pH from 6.0-9.5
9566
8.5 - 12
Q308C1;
very stable in alkaline buffer
701082
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
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half-life: 50 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes
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Mg2+ stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
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-20°C, protein concentration 50 mg/ml, 50% v/v glycerol, stable 3 months, loss of activity less than 50%
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4°C, 100 mM Tris/HCl buffer, 2 mM 2-mercaptoethanol, 50 days
Q308C1;
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol for 50 days, 50% loss of activity. Addition of 2-mercaptoethanol is required
Q308C1;
frozen after second calcium phosphate gel preparation, stable for 3 years
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
Q308C1;
recombinant protein from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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)
Q308C1;
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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induced by D-arabinitol
Q308C1;
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the gene can be expressed in agronomic plants to withstand abiotic stresses
analysis
biotechnology
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the gene can be expressed in agronomic plants to withstand abiotic stresses
industry
Q308C1;
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