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

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EC NUMBER
COMMENTARY hide
1.1.1.287
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RECOMMENDED NAME
GeneOntology No.
D-arabinitol dehydrogenase (NADP+)
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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
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
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-
Metabolic pathways
-
-
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivated on artificial surfaces in in vitro infection structures
SwissProt
Manually annotated by BRENDA team
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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
?
-
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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
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
Q308C1
NADH is preferred over NADPH
NADP+
NADPH
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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+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
Q308C1
10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA
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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
-
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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
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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
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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
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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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
Q308C1
ketone reduction
8.5
Q308C1
polyol oxidation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
Q308C1
2% of maximum activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
Q308C1
isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
exclusively, in the lumen
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
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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
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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
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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
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by growth on D-arabinitol
Q308C1
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inhibition by Cu2+ can partly be restored by EDTA
Q308C1
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.287)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)