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Enzyme Nomenclature
Information on EC 1.1.1.11 - D-arabinitol 4-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.11
Word Map on EC 1.1.1.11
- 1.1.1.11
- xylitol
- gluconobacter
- ribitol
-
polyols
- d-mannitol
- d-sorbitol
- suboxydans
- pentitols
-
nad-dependent
-
klebsiella
- d-ribulose
- oxydans
-
quinoproteins
- d-xylose
- acetobacter
-
oxidoreduction
- 5-keto-d-gluconate
- d-xylulokinase
- l-xylulose
-
2-dehydrogenase
-
ketopentose
- meso-erythritol
- aerogenes
- erythritol
- d-gluconate
- pqq
- analysis
- industry
- biotechnology
- agriculture
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.11
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RECOMMENDED NAME
GeneOntology No.
D-arabinitol 4-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NAD+ = D-xylulose + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
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SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 4-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-18-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
D-arabitol + NAD+
D-xylulose + NADH + H+
is the optimal substrate for aArDH
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r
D-glucitol + NAD+
?
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recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
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-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
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recombinant protein from Saccharomyces cerevisiae
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?
D-arabinitol + NAD+
D-xylulose + NADH + H+
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D-arabitol i.e. D-arabinitol
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Galactitol + NAD+
?
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recombinant protein from Saccharomyces cerevisiae
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-
?
Xylitol + NAD+
?
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recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
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?
additional information
?
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both purified native and recombinant aArDH do not accept L-arabitol as substrate
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additional information
?
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both purified native and recombinant aArDH do not accept L-arabitol as substrate
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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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D-arabinitol + NAD+
D-ribulose + NADH + H+
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recombinant protein from Saccharomyces cerevisiae
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?
D-arabinitol + NAD+
D-xylulose + NADH + H+
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D-arabitol i.e. D-arabinitol
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
aArDH prefers NAD+ to NADP+ as coenzyme; NAD+ is preferred over NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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no divalent cations are required for activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68.5
pH 8.5, 25°C; recombinant aArDH with 100 mM D-arabitol as substrate
additional information
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grown on medium with D-arabinitol, specific activity of crude cell extract: 1.13-3.47
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
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pH 6.0: about 60% of maximum activity, pH 8.5: about 60% of activity maximum
10 - 11
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enzyme activity increases with increasing pH, measurements above pH 11.0 not feasible
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28500
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
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4 * 30000, calculated from gene sequence and molecular weight of native enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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 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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
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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)
gene over-expressed in S. cerevisiae BWG 1-7A and in Escherichia coli JM109, DH5-alpha
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.11)
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