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EC Tree
IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ARD1p, ArDH, D-arabitol dehydrogenase, D-arabitol dehydrogenase 1, More, NADP(+)-dependent D-arabitol dehydrogenase,
more
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D-arabitol dehydrogenase 1
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NADP(+)-dependent D-arabitol dehydrogenase
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ArDH
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D-arabitol dehydrogenase
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D-arabitol dehydrogenase
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additional information
the enzyme belongs to the short-chain dehydrogenase family
additional information
the enzyme belongs to the short-chain dehydrogenase family
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D-arabinitol + NADP+ = D-ribulose + NADPH + H+
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-
-
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D-arabinitol + NADP+ = D-xylulose + NADPH + H+
-
-
-
-
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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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D-arabitinol + NADP+
D-ribulose + NADPH
-
-
-
r
D-arabitinol + NADP+
D-xylulose + NADPH
D-arabitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
D-arabitol + NADP+
D-xylulose + NADPH + H+
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-mannitol + NADP+
D-fructose + NADPH + H+
D-ribitol + NAD+
D-ribulose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
sorbose + NADH + H+
-
-
-
?
D-sorbitol + NADP+
sorbose + NADPH
D-xylulose + NAD+
D-arabitol + NADH
-
-
-
r
glycerol + NAD+
dihydroxyacetone + NADH
-
-
-
?
glycerol + NADP+
? + NADPH
-
-
-
r
meso-erythritol + NADP+
L-erythrose + NADPH
-
-
-
r
xylitol + NAD+
D-xylulose + NADH
-
-
-
?
additional information
?
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D-arabitinol + NADP+
D-xylulose + NADPH
-
-
-
?
D-arabitinol + NADP+
D-xylulose + NADPH
-
-
-
?
D-arabitinol + NADP+
D-xylulose + NADPH
-
-
-
r
D-arabitol + NADP+
D-xylulose + NADPH + H+
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-
-
r
D-arabitol + NADP+
D-xylulose + NADPH + H+
preferred substrate for the forward and reverse reaction, respectively
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-
r
D-arabitol + NADP+
D-xylulose + NADPH + H+
preferred substrate for the forward and reverse reaction, respectively
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-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
preferred substrate for the forward and reverse reaction, respectively
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-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
preferred substrate for the forward and reverse reaction, respectively
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-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
-
-
-
r
D-sorbitol + NADP+
sorbose + NADPH
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-
-
r
D-sorbitol + NADP+
sorbose + NADPH
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-
-
r
additional information
?
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substrate specificity for different sugars, overview, no activity with xylitol, L-arabitol, and L-sorbitol
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-
?
additional information
?
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substrate specificity for different sugars, overview, no activity with xylitol, L-arabitol, and L-sorbitol
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-
?
additional information
?
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the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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?
additional information
?
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the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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?
additional information
?
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the enzyme shows high substrate specificity, the reverse reaction is preferred
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-
?
additional information
?
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the enzyme shows high substrate specificity, the reverse reaction is preferred
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-
?
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D-arabitinol + NADP+
D-xylulose + NADPH
additional information
?
-
D-arabitinol + NADP+
D-xylulose + NADPH
-
-
-
?
D-arabitinol + NADP+
D-xylulose + NADPH
-
-
-
?
additional information
?
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the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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-
?
additional information
?
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the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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-
?
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NADH
NADH is preferred over NADPH
NADP+
dependent on
NADP+
dependent on, absolutely specific for, forward reaction
NADPH
dependent on, absolutely specific for, reverse reaction
NADPH
NADH is preferred over NADPH
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Ba2+
up to 200 mM, 2fold increase in activity
Ca2+
up to 200 mM, 2fold increase in activity
additional information
no effect by addition of Mn2+, Ni2+, Mg2+
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Cu2+
10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA
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242.8
D-ribitol
pH 8.5, 25°C
266
meso-erythritol
pH 8.5, 25°C
18.5
xylitol
pH 8.5, 25°C
additional information
additional information
-
4.5
D-arabitol
pH 8.5, 25°C
12.5
D-arabitol
pH 8.5, 25°C
47
D-fructose
pH 6.0, 25°C
18.5
D-mannitol
pH 8.5, 25°C
78.5
D-mannitol
pH 8.5, 25°C
125
D-sorbitol
pH 8.5, 25°C
127.3
D-sorbitol
pH 8.5, 25°C
7.8
D-xylulose
pH 6.0
25
D-xylulose
pH 6.0, 25°C
133.6
glycerol
pH 8.5, 25°C
384
glycerol
pH 8.5, 25°C
0.07
NADP+
pH 9.0, with D-mannitol
0.08
NADP+
pH 9.0, with D-arabitinol
0.16
NADPH
pH 6.0, with D-fructose
0.2
NADPH
pH 6.0, with D-ribulose
0.26
NADPH
pH 6.0, with D-xylulose
additional information
additional information
kinetics
-
additional information
additional information
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kinetics
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224
D-fructose
pH 6.0, 25°C
13.4
D-ribitol
pH 8.5, 25°C
196
D-xylulose
pH 6.0, 25°C
1.28
meso-erythritol
pH 8.5, 25°C
177.2
xylitol
pH 8.5, 25°C
258
D-arabitol
pH 8.5, 25°C
876
D-arabitol
pH 8.5, 25°C
35.3
D-mannitol
pH 8.5, 25°C
243
D-mannitol
pH 8.5, 25°C
2.57
D-sorbitol
pH 8.5, 25°C
19.7
D-sorbitol
pH 8.5, 25°C
1.33
glycerol
pH 8.5, 25°C
16.3
glycerol
pH 8.5, 25°C
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194.7
D-arabitol
pH 8.5, 25°C
0.45
D-mannitol
pH 8.5, 25°C
0.06
D-ribitol
pH 8.5, 25°C
0.15
D-sorbitol
pH 8.5, 25°C
0.12
glycerol
pH 8.5, 25°C
9.58
xylitol
pH 8.5, 25°C
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11.4
purified recombinant enzyme, substrate D-xylulose
12.6
substrate D-xylitol, pH 8.5, 25°C
16.4
substrate D-xylulose, pH 5.5, 25°C
2.8
purified recombinant enzyme, substrate glycerol
23.5
purified recombinant enzyme, substrate D-mannitol
27.6
purified recombinant enzyme, substrate D-arabitol
3.2
purified recombinant enzyme, substrate meso-erythritol
6.4
purified recombinant enzyme, substrate D-sorbitol
68.5
substrate D-arabitol, pH 8.5, 25°C
7.9
purified recombinant enzyme, substrate D-fructose
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6
assay at, reverse reaction
9
assay at, forward reaction
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50
2% of maximum activity
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SwissProt
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cultivated on artificial surfaces in in vitro infection structures
SwissProt
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SwissProt
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UniProt
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exclusively, in the lumen
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-
-
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additional information
cultivated on artificial surfaces in in vitro infection structures
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additional information
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cultivated on artificial surfaces in in vitro infection structures
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-
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bound
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bound
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ARD1_UROFA
349
0
38372
Swiss-Prot
other Location (Reliability: 2 )
A0A087ECB9_9BIFI
380
0
41447
TrEMBL
-
A0A7W8C907_9MYCO
341
0
35739
TrEMBL
-
A0A076JK85_9BIFI
342
0
36926
TrEMBL
-
A0A212KEA2_9FIRM
339
0
36836
TrEMBL
-
A0A7X5R028_9MICO
340
0
35830
TrEMBL
-
A0A483BDG5_OENOE
337
0
36441
TrEMBL
-
A0A084G7A3_PSEDA
336
0
36482
TrEMBL
other Location (Reliability: 2 )
A0A087BDK5_9BIFI
334
0
35697
TrEMBL
-
A0A087A928_9BIFI
334
0
35687
TrEMBL
-
A0A087CFI1_9BIFI
335
0
35616
TrEMBL
-
A0A087DD80_9BIFI
375
0
40866
TrEMBL
-
A0A7W5P7S7_9ACTN
344
0
35875
TrEMBL
-
A0A7X5TSZ3_9MICO
351
0
36810
TrEMBL
-
A0A087DLU4_BIFAD
334
0
35913
TrEMBL
-
A0A087VW63_9BIFI
342
0
36920
TrEMBL
-
A0A087DSX7_9BIFI
334
0
35882
TrEMBL
-
A0A087CWB7_9BIFI
334
0
35713
TrEMBL
-
Q308C1_GLUOY
257
0
27552
TrEMBL
-
Q58LW6_GLUOY
257
0
27497
TrEMBL
-
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140000
gel filtration, native enzyme
29000
x * 29000, recombinant enzyme, SDS-PAGE
70000
gel filtration, recombinant enzyme
28500
2 * 28500, SDS-PAGE and calculated, recombinant enzyme
28500
4 * 28500, SDS-PAGE and calculated, native enzyme
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dimer
2 * 28500, SDS-PAGE and calculated, recombinant enzyme
tetramer
4 * 28500, SDS-PAGE and calculated, native enzyme
?
x * 29000, recombinant enzyme, SDS-PAGE
?
-
x * 29000, recombinant enzyme, SDS-PAGE
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4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol, 50 days, 50% oxidative activity
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol, 80 days, 5% oxidative activity
4°C, 100 mM Tris/HCl without 2 mM 2-mercaptoethanol, 20 days, complete loss of activity
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli
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expression in Escherichia coli
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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induced by growth on D-arabinitol
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inhibition by Cu2+ can partly be restored by EDTA
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Link, T.; Lohaus, G.; Heiser, I.; Mendgen, K.; Hahn, M.; Voegele, R.T.
Characterization of a novel NADP(+)-dependent D-arabitol dehydrogenase from the plant pathogen Uromyces fabae
Biochem. J.
389
289-295
2005
Uromyces viciae-fabae (Q4R0J7), Uromyces viciae-fabae
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Cheng, H.; Jiang, N.; Shen, A.; Feng, Y.
Molecular cloning and functional expression of D-arabitol dehydrogenase gene from Gluconobacter oxydans in Escherichia coli
FEMS Microbiol. Lett.
252
35-42
2005
Gluconobacter oxydans (Q58LW6), Gluconobacter oxydans CGMCC 1.110 (Q58LW6)
brenda
Cheng, H.; Li, Z.; Jiang, N.; Deng, Z.
Cloning, purification and characterization of an NAD-dependent D-arabitol dehydrogenase from acetic acid bacterium, Acetobacter suboxydans
Protein J.
28
263-272
2009
Gluconobacter oxydans (Q308C1)
brenda
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