Any feedback?
No. of entries
Information on EC 1.1.1.11 - D-arabinitol 4-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.11 D-arabinitol 4-dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
d-arabitol dehydrogenase, arabitol dehydrogenase, d-xylulose-forming d-arabitol dehydrogenase, aardh, nad-dependent d-arabitol dehydrogenase, d-arabinitol 4-dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arabitol dehydrogenase
D-arabitol dehydrogenase
dehydrogenase, D-arabinitol
-
-
-
-
arabitol dehydrogenase
-
-
-
-
D-arabitol dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NAD+ = D-xylulose + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
D-arabinitol degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 4-oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-18-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose + NADH + H+
D-mannitol + NAD+
Substrates: -
Products: -
Products: -
?
D-glucitol + NAD+
?
-
Substrates: recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
Products: -
Products: -
?
D-ribulose + NADH + H+
D-arabinitol + NAD+
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-sorbitol + NAD+
sorbose + NADH + H+
Gluconobacter sp. JX-05
Substrates: 10.3% activity with D-sorbitol compared to D-arabitol
Products: -
Products: -
r
D-xylulose + NADH + H+
D-arabitol + NAD+
Substrates: -
Products: -
Products: -
r
meso-erythritol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
meso-erythritol + NAD+
L-erythrose + NADH + H+
Gluconobacter sp. JX-05
Substrates: 5.3% activity with D-sorbitol compared to D-arabitol
Products: -
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
Substrates: recombinant protein from Saccharomyces cerevisiae
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: D-arabitol i.e. D-arabinitol
Products: -
Products: -
?
D-arabitol + NAD+
D-xylulose + NADH + H+
Substrates: is the optimal substrate for aArDH
Products: -
Products: -
r
D-arabitol + NAD+
D-xylulose + NADH + H+
Gluconobacter sp. JX-05
Substrates: best substrates in both reaction directions
Products: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-mannitol + NAD+
D-fructose + NADH + H+
Gluconobacter sp. JX-05
Substrates: 30.5% and 54.8% activity with D-mannitol and D-fructose compared to D-arabitol and D-xylulose, respectively
Products: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
ethanol + NAD+
acetaldehyde + NADH + H+
Gluconobacter sp. JX-05
Substrates: 1.9% activity with D-sorbitol compared to D-arabitol
Products: -
Products: -
?
Galactitol + NAD+
?
-
Substrates: recombinant protein from Saccharomyces cerevisiae
Products: -
Products: -
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
Substrates: -
Products: -
Products: -
?
glycerol + NAD+
dihydroxyacetone + NADH + H+
Gluconobacter sp. JX-05
Substrates: 6.2% activity with D-sorbitol compared to D-arabitol
Products: -
Products: -
?
Xylitol + NAD+
?
-
Substrates: recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Gluconobacter sp. JX-05
Substrates: 8.8% activity with D-sorbitol compared to D-arabitol
Products: -
Products: -
r
additional information
?
-
-
Substrates: no activity with D-mannitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: both purified native and recombinant aArDH do not accept L-arabitol as substrate
Products: -
Products: -
?
additional information
?
-
Substrates: both purified native and recombinant aArDH do not accept L-arabitol as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: L-arabinitol
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: L-arabinitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribulose + NADH + H+
D-arabinitol + NAD+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
Products: -
Products: -
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
Substrates: recombinant protein from Saccharomyces cerevisiae
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
Substrates: D-arabitol i.e. D-arabinitol
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
Gluconobacter sp. JX-05
the enzyme harbors the NAD(P)-binding motif TGXXXGXG, preferred substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no divalent cations are required for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.7
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates ethanol and NAD+, recombinant His-tagged enzyme
12.6
22.9
Gluconobacter sp. JX-05
pH 5.5, 30°C, substrates D-xylulose and NADH, recombinant His-tagged enzyme
26.8
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates D-mannitol and NAD+, recombinant His-tagged enzyme
4.7
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates meso-erythritol and NAD+, recombinant His-tagged enzyme
5.5
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates glycerol and NAD+, recombinant His-tagged enzyme
68.5
7.7
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates xylitol and NAD+, recombinant His-tagged enzyme
87.7
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates D-arabitol and NAD+, recombinant His-tagged enzyme
9
Gluconobacter sp. JX-05
pH 8.5, 30°C, substrates D-sorbitol and NAD+, recombinant His-tagged enzyme
additional information
-
grown on medium with D-arabinitol, specific activity of crude cell extract: 1.13-3.47
12.6
Gluconobacter sp. JX-05
pH 5.5, 30°C, substrates D-fructose and NADH, recombinant His-tagged enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
8.5
8.5
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 11
-
enzyme activity increases with increasing pH, measurements above pH 11.0 not feasible
3 - 7
Gluconobacter sp. JX-05
reduction of D-xylulose with NADH, over 80% of maximal activity within this range, recombinant His-tagged enzyme
6 - 11
Gluconobacter sp. JX-05
oxidation of D-arabitol with NAD+, over 60% of maximal activity within this range, recombinant His-tagged enzyme
6 - 8.5
-
pH 6.0: about 60% of maximum activity, pH 8.5: about 60% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 55
Gluconobacter sp. JX-05
oxidation and reduction activities of ArDH, over 80% of maximal activity at 24-40°C, and below 60% of maximal activity when the temperature exceeds 55°C, recombinant His-tagged enzyme
30 - 50
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Klebsiella pneumoniae, gene expression in Escherichia coli K12
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Gluconobacter sp. JX-05
enzyme ArDH containing a NAD(P)-binding motif TGXXX[AG]XG and a classical active site motif belongs to the short-chain dehydrogenase family
additional information
Gluconobacter sp. JX-05
ArDH has a conserved sequence region of TGXXXGXG, in this NAD(P)-binding motif, glycine-rich region plays a critical role in the stability of this kind of domain. Conserved domain of YXXXK, a classical active site motif, accompanying with two conserved amino acids N119 and S147 in the upstream, is also found in ArDH, sequence comparisons. Structure-function analysis of ArDH, and structure homology modeling using the structure of putative polyol dehydrogenase (PDB ID 3AWD) from Gluconobacter oxydans strain DSM2343 as template, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). DALD_KLEPN
455
0
51022
Swiss-Prot
Mitochondrion (Reliability: 3)
DALD_RALN1
Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000)
465
0
50630
Swiss-Prot
-
Q308C1_GLUOY
257
0
27552
TrEMBL
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28500
30000
-
4 * 30000, calculated from gene sequence and molecular weight of native enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
4 * 30000, calculated from gene sequence and molecular weight of native enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Gluconobacter sp. JX-05
in the co-biotransformation by the whole cells of recombinant Escherichia coli BL21(DE3)-ardh and BL21(DE3)-xdh strains, 26.1 g/l xylitol is produced from 30 g/l D-arabitol in 22 h with a yield 0.87 g/g. The xylitol production is increased by more than two times as compared with that of Gluconobacter sp. alone, and is improved 10.1% than that of Gluconobacter sp. mixed with Escherichia coli strain BL21(DE3)-xdh
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Gluconobacter sp. JX-05
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression vector containing the ORF of aArDH under the control of T7 promoter, pET21aArDH, transformed into Escherichia coli strain BL21(DE3)
gene ardh, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Gluconobacter sp. JX-05
gene over-expressed in S. cerevisiae BWG 1-7A and in Escherichia coli JM109, DH5-alpha
-
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
-
recombinant expression of the yeast enzyme in Nicotiana tabacum using the chloroplast transformation vector pMSK83 harboring aadA and ArDH genes under the control of chloroplast regulatory sequences
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ArDH enzyme expression in tobacco chloroplasts confers tolerance to NaCl (up to 400 mM). Transgenic plants compared to wild-type survived for only 4-5 weeks on 400 mM NaCl whereas plants remain green and grow normal on concentrations up to 350 mM NaCl. A-week-old seedlings are also challenged with PEG up to 6% in the liquid medium, considering that membranes and proteins are protected under stress conditions due to accumulation of arabitol in chloroplasts. Seedlings are tolerant to 6% PEG, suggesting that ARDH enzyme maintains integrity of membranes in chloroplasts under drought conditions via metabolic engineering
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
the gene can be expressed in agronomic plants to withstand abiotic stresses
analysis
biotechnology
-
the gene can be expressed in agronomic plants to withstand abiotic stresses
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
analysis
-
potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker
analysis
-
potential of using arabitol dehydrogenase from the non-virulent enteric bacterium, Escherichia colistrain C, as a plant selectable marker
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wong, B.; Murray, J.S.; Castellanos, M.; Croen, K.D.
D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase
J. Bacteriol.
175
6314-6320
1993
Candida albicans, Candida albicans B331
brenda
Quong, M.W.; Miyada, C.G.; Switchenko, A.C.; Goodman, T.C.
Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis
Biochem. Biophys. Res. Commun.
196
1323-1329
1993
Candida tropicalis
brenda
Neuberger, M.S.; Patterson, R.A.; Hartley, B.S.
Purification and properties of Klebsiella aerogenes D-arabitol dehydrogenase
Biochem. J.
183
31-42
1979
Klebsiella aerogenes
brenda
Wilson, B.L.; Mortlock, R.P.
Regulation of D-xylose and D-arabitol catabolism by Aerobacter aerogenes
J. Bacteriol.
113
1404-1411
1973
Klebsiella aerogenes, Klebsiella aerogenes PRL-R3
brenda
Fossitt, D.D.; Wood, W.A.
D-Arabitol dehydrogenase
Methods Enzymol.
9
184-187
1966
Klebsiella aerogenes, Klebsiella aerogenes PRL-R3
-
brenda
Wood, W.A.; McDonough, M.J.; Jacobs, L.B.
Ribitol and D-arabitol utilization by Aerobacter aerogenes
J. Biol. Chem.
236
2190-2195
1961
Klebsiella aerogenes, Klebsiella aerogenes PRL-R3
brenda
Lin, E.C.C.
An inducible D-arabitol dehydrogenase from Aerobacter aerogenes
J. Biol. Chem.
236
31-36
1961
Klebsiella aerogenes
brenda
Murray, J.S.; Wong, M.L.; Miyada, C.G.; Switchenko, A.C.; Goodman, T.C.; Wong, B.
Isolation, characterization and expression of the gene that encodes D-arabinitol dehydrogenase in Candida tropicalis
Gene
155
123-128
1995
Candida tropicalis
brenda
Hallborn, J.; Walfridsson, M.; Penttilae, M.; Keraenen, S.; Hahn-Haegerdal, B.
A short-chain dehydrogenase gene from Pichia stipitis having D-arabinitol dehydrogenase activity
Yeast
11
839-847
1995
Scheffersomyces stipitis
brenda
LaFayette, P.R.; Kane, P.M.; Phan, B.H.; Parrott, W.A.
Arabitol dehydrogenase as a selectable marker for rice
Plant Cell Rep.
24
596-602
2005
Escherichia coli, Escherichia coli C
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, Gluconobacter oxydans (Q308C1)
brenda
Khan, M.S.; Kanwal, B.; Nazir, S.
Metabolic engineering of the chloroplast genome reveals that the yeast ArDH gene confers enhanced tolerance to salinity and drought in plants
Front. Plant Sci.
6
725
2015
Saccharomyces cerevisiae
brenda
Qi, X.; Zhang, H.; Magocha, T.A.; An, Y.; Yun, J.; Yang, M.; Xue, Y.; Liang, S.; Sun, W.; Cao, Z.
Improved xylitol production by expressing a novel D-arabitol dehydrogenase from isolated Gluconobacter sp. JX-05 and co-biotransformation of whole cells
Biores. Technol.
235
50-58
2017
Gluconobacter sp. JX-05 (A0A2K9VPX3)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.11)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
