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Information on EC 1.1.1.287 - D-arabinitol dehydrogenase (NADP+)
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1.1.1.287 D-arabinitol dehydrogenase (NADP+)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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Synonyms
ARD1p, ArDH, D-arabitol dehydrogenase, D-arabitol dehydrogenase 1, More, NADP(+)-dependent D-arabitol dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ArDH
D-arabitol dehydrogenase
additional information
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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NADP+ = D-ribulose + NADPH + H+
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D-arabinitol + NADP+ = D-xylulose + NADPH + H+
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PATHWAY SOURCE
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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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 + 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
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
?
-
substrate specificity for different sugars, overview, no activity with xylitol, L-arabitol, and L-sorbitol
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-
?
additional information
?
-
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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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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-
?
additional information
?
-
-
the enzyme activity is highly increased during infection processes and pathogenesis, development after infection, overview
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no effect by addition of Mn2+, Ni2+, Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivated on artificial surfaces in in vitro infection structures
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cultivated on artificial surfaces in in vitro infection structures
brenda
additional information
-
cultivated on artificial surfaces in in vitro infection structures
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ARD1_UROFA
349
0
38372
Swiss-Prot
other Location (Reliability: 2)
A0A212KEA2_9FIRM
339
0
36836
TrEMBL
-
A0A087DD80_9BIFI
375
0
40866
TrEMBL
-
A0A087DSX7_9BIFI
334
0
35882
TrEMBL
-
A0A084G7A3_PSEDA
336
0
36482
TrEMBL
other Location (Reliability: 2)
A0A087VW63_9BIFI
342
0
36920
TrEMBL
-
A0A087A928_9BIFI
334
0
35687
TrEMBL
-
A0A087CFI1_9BIFI
335
0
35616
TrEMBL
-
A0A087DLU4_BIFAD
334
0
35913
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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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