Information on EC 1.1.1.287 - D-arabinitol dehydrogenase (NADP+)

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

EC NUMBER
COMMENTARY hide
1.1.1.287
-
RECOMMENDED NAME
GeneOntology No.
D-arabinitol dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NADP+ = D-ribulose + NADPH + H+
show the reaction diagram
-
-
-
-
D-arabinitol + NADP+ = D-xylulose + NADPH + H+
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NADP+ oxidoreductase
The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. This enzyme carries out the reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC 1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+ rather than NAD+ as cofactor. D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivated on artificial surfaces in in vitro infection structures
SwissProt
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-arabitinol + NADP+
D-ribulose + NADPH
show the reaction diagram
-
-
-
r
D-arabitinol + NADP+
D-xylulose + NADPH
show the reaction diagram
D-arabitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
D-arabitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
D-mannitol + NADP+
D-fructose + NADPH + H+
show the reaction diagram
D-ribitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
D-sorbitol + NAD+
sorbose + NADH + H+
show the reaction diagram
Q308C1;
-
-
-
?
D-sorbitol + NADP+
sorbose + NADPH
show the reaction diagram
D-xylulose + NAD+
D-arabitol + NADH
show the reaction diagram
Q308C1;
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
show the reaction diagram
Q308C1;
-
-
-
?
glycerol + NADP+
? + NADPH
show the reaction diagram
-
-
-
r
meso-erythritol + NADP+
L-erythrose + NADPH
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH
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-arabitinol + NADP+
D-xylulose + NADPH
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
Q308C1;
NADH is preferred over NADPH
NADP+
NADPH
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
additional information
Q308C1;
no effect by addition of Mn2+, Ni2+, Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
Q308C1;
10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
834
D-arabitinol
pH 9.0
4.5 - 12.5
D-arabitol
47 - 160
D-fructose
18.5 - 425
D-mannitol
242.8
D-ribitol
Q308C1;
pH 8.5, 25°C
53.9
D-ribulose
pH 6.0
125 - 127.3
D-sorbitol
7.8 - 25
D-xylulose
133.6 - 384
glycerol
266
meso-erythritol
pH 8.5, 25°C
0.07 - 0.08
NADP+
0.16 - 0.26
NADPH
18.5
xylitol
Q308C1;
pH 8.5, 25°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
258 - 876
D-arabitol
224
D-fructose
pH 6.0, 25°C
35.3 - 243
D-mannitol
13.4
D-ribitol
Q308C1;
pH 8.5, 25°C
2.57 - 19.7
D-sorbitol
196
D-xylulose
pH 6.0, 25°C
1.33 - 16.3
glycerol
1.28
meso-erythritol
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-arabitol
Q308C1;
pH 8.5, 25°C
0.45
D-mannitol
Q308C1;
pH 8.5, 25°C
0.06
D-ribitol
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
9.58
xylitol
Q308C1;
pH 8.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
purified recombinant enzyme, substrate glycerol
3.2
purified recombinant enzyme, substrate meso-erythritol
6.4
purified recombinant enzyme, substrate D-sorbitol
7.9
purified recombinant enzyme, substrate D-fructose
11.4
purified recombinant enzyme, substrate D-xylulose
12.6
Q308C1;
substrate D-xylitol, pH 8.5, 25°C
16.4
Q308C1;
substrate D-xylulose, pH 5.5, 25°C
23.5
purified recombinant enzyme, substrate D-mannitol
27.6
purified recombinant enzyme, substrate D-arabitol
68.5
Q308C1;
substrate D-arabitol, pH 8.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
assay at, reverse reaction
6.5
reverse reaction
8.5
forward reaction
9
assay at, forward reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
Q308C1;
ketone reduction
8.5
Q308C1;
polyol oxidation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
Q308C1;
2% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
Q308C1;
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
exclusively, in the lumen
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28500
Q308C1;
2 * 28500, SDS-PAGE and calculated, recombinant enzyme; 4 * 28500, SDS-PAGE and calculated, native enzyme
29000
x * 29000, recombinant enzyme, SDS-PAGE
70000
Q308C1;
gel filtration, recombinant enzyme
140000
Q308C1;
gel filtration, native enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
Q308C1;
2 * 28500, SDS-PAGE and calculated, recombinant enzyme
tetramer
Q308C1;
4 * 28500, SDS-PAGE and calculated, native enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol, 50 days, 50% oxidative activity
Q308C1;
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol, 80 days, 5% oxidative activity
Q308C1;
4°C, 100 mM Tris/HCl without 2 mM 2-mercaptoethanol, 20 days, complete loss of activity
Q308C1;
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme
Q308C1;
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q308C1;
gene ARD1, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae strain 23344c, overexpression in Escherichia coli strain BL21(DE3) as N-terminally His6-tagged protein
gene ArDH, DNA and amino acid sequence determination and analysis, gene ArDH is part of an operon with several components of a sugar transporter system, subcloning in Escherichia coli strain TG-1, functional expression in Escherichia coli strain BL21(DE3) as His6-tagged enzyme
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by growth on D-arabinitol
Q308C1;
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inhibition by Cu2+ can partly be restored by EDTA
Q308C1;