Information on EC 1.1.1.11 - D-arabinitol 4-dehydrogenase

Word Map on EC 1.1.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-arabitol degradation
-
-
Fructose and mannose metabolism
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
degradation of sugar alcohols
-
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 4-oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-18-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain B331, WO-1, 1006, 1001
-
-
Manually annotated by BRENDA team
strain B331, WO-1, 1006, 1001
-
-
Manually annotated by BRENDA team
strain C
-
-
Manually annotated by BRENDA team
strain C
-
-
Manually annotated by BRENDA team
strain CBS 6054
-
-
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
is the optimal substrate for aArDH
-
-
r
D-fructose + NADH + H+
D-mannitol + NAD+
show the reaction diagram
-
-
-
?
D-glucitol + NAD+
?
show the reaction diagram
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
-
-
-
?
D-xylulose + NADH + H+
D-arabitol + NAD+
show the reaction diagram
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
-
-
-
?
Galactitol + NAD+
?
show the reaction diagram
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
-
-
-
?
L-Xylulose + NADH
?
show the reaction diagram
-
3% activity
-
-
?
meso-erythritol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
-
-
-
?
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
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
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
D-arabinitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
; NAD+ is preferred over NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arabitol
inducer
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 39.8
D-arabinitol
6.1 - 78.5
D-mannitol
127.3
D-sorbitol
; pH 8.5, 25°C
1.14 - 2
D-xylulose
133.6
glycerol
; pH 8.5, 25°C
0.04 - 0.2
NAD+
242.8
ribitol
; pH 8.5, 25°C
18.5 - 177.2
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
876
D-arabinitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
876
D-arabitol
Gluconobacter oxydans
Q308C1
-
35.3
D-mannitol
Gluconobacter oxydans
Q308C1
; pH 8.5, 25°C
19.7
D-sorbitol
Gluconobacter oxydans
Q308C1
; pH 8.5, 25°C
16.3
glycerol
Gluconobacter oxydans
Q308C1
; pH 8.5, 25°C
13.4
ribitol
Gluconobacter oxydans
Q308C1
; pH 8.5, 25°C
177.2
xylitol
Gluconobacter oxydans
Q308C1
; pH 8.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
194.7
D-arabinitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
2268
0.45
D-mannitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
495
0.15
D-sorbitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
627
0.12
glycerol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
135
0.06
ribitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
1476
9.58
xylitol
Gluconobacter oxydans
Q308C1
pH 8.5, 25°C
416
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.14
crude extract
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
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
4.2
recombinant aArDH with D-mannitol as substrate
12.6
recombinant aArDH with xylitol as substrate
16.4
recombinant aArDH with D-xylulose as substrate
16.66
119fold purified enzyme
68.25
-
D-arabinitol, of recombinant protein
68.5
pH 8.5, 25°C; recombinant aArDH with 100 mM D-arabitol as substrate
187
-
of recombinant protein
additional information
-
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
optimum for ketone reduction
6.5
-
optimal activity, reduction
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
9
-
D-arabinitol, D-mannitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
10 - 11
-
enzyme activity increases with increasing pH, measurements above pH 11.0 not feasible
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
enzyme assay at
28
-
enzyme assay at
30
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
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
isoelectric focusing
5.9
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
4 * 28500, calculated, 4 * 28000, SDS-PAGE
28500
4 * 28500, calculated, 4 * 28000, SDS-PAGE; native aArDH, 2 * 28500, SDS-PAGE; recombinant aArDH, 2 * 28500, 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
110000
-
native gradient PAGE
140000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
native aArDH, 2 * 28500, SDS-PAGE
homodimer
recombinant aArDH, 2 * 28500, SDS-PAGE
monomer
-
1 * 46500, SDS-PAGE
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
more labile at increasing pH from 6.0-9.5
9566
8.5 - 12
very stable in alkaline buffer
701082
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
-
half-life: 50 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes
-
Mg2+ stabilizes
-
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
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
recombinant protein from Escherichia coli
-
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 Escherichia coli BW31M
-
gene over-expressed in Escherichia coli K12
-
gene over-expressed in S. cerevisiae BWG 1-7A and in Escherichia coli JM109, DH5-alpha
-
gene over-expressed in Saccharomyces cerevisiae S700
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by D-arabinitol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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