HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.1.11 - D-arabinitol 4-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.11 D-arabinitol 4-dehydrogenaseSpecify your search results
Word Map
- 1.1.1.11
- xylitol
- gluconobacter
- ribitol
- d-mannitol
- pentitols
-
nad-dependent
- suboxydans
- polyols
- d-sorbitol
- d-xylose
- acetobacter
-
quinoproteins
- oxydans
- d-ribulose
- industry
- biotechnology
- agriculture
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aArDH, arabitol dehydrogenase, D-arabitol dehydrogenase, D-xylulose-forming D-arabitol dehydrogenase, dehydrogenase, D-arabinitol, 
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
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
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 + NAD+
D-xylulose + NADH + H+
is the optimal substrate for aArDH
-
-
r
D-glucitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
-
-
?
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
recombinant protein from Saccharomyces cerevisiae
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
D-arabitol i.e. D-arabinitol
-
-
Galactitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae
-
-
?
Xylitol + NAD+
?
-
recombinant protein from Saccharomyces cerevisiae and enzyme from Pichia stipitis
-
-
?
additional information
?
-
-
both purified native and recombinant aArDH do not accept L-arabitol as substrate
-
-
-
additional information
?
-
both purified native and recombinant aArDH do not accept L-arabitol as substrate
-
-
-
additional information
?
-
-
D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
-
-
-
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
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
?
-
-
D-arabinitol dehydrogenases (ArDH) from fungi and yeast oxidize D-arabinitol to D-ribulose, whereas bacterial ArDH oxidizes D-arabinitol to D-xylulose
-
-
-
D-arabinitol + NAD+
D-ribulose + NADH + H+
-
recombinant protein from Saccharomyces cerevisiae
-
?
D-arabinitol + NAD+
D-xylulose + NADH + H+
-
D-arabitol i.e. D-arabinitol
-
-
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+
aArDH prefers NAD+ to NADP+ as coenzyme; NAD+ is preferred over NADP+
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
68.5
pH 8.5, 25°C; recombinant aArDH with 100 mM D-arabitol as substrate
additional information
-
grown on medium with D-arabinitol, specific activity of crude cell extract: 1.13-3.47
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
optimum for polyol oxidation; 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
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
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
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
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
DALD_RALSO
Ralstonia solanacearum (strain GMI1000)
465
0
50630
Swiss-Prot
A0A0P0R4M1_9BURK
469
0
51611
TrEMBL
A0A1B7K280_9GAMM
462
0
52536
TrEMBL
F0Q9M3_ACIAP
Acidovorax avenae (strain ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011)
464
0
50800
TrEMBL
A2QK54_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
267
0
28781
TrEMBL
A2R6B7_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
509
0
57781
TrEMBL
Q39DF6_BURL3
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
464
0
50590
TrEMBL
D8IX95_HERSS
Herbaspirillum seropedicae (strain SmR1)
477
0
52529
TrEMBL
C9YC84_9BURK
468
0
51436
TrEMBL
B2VCG7_ERWT9
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
467
0
52043
TrEMBL
A0A0N0I9P8_9GAMM
472
0
53418
TrEMBL
B4E9J7_BURCJ
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
464
0
50389
TrEMBL
A0A1B7INE1_9ENTR
455
0
50880
TrEMBL
Q13UN5_PARXL
Paraburkholderia xenovorans (strain LB400)
470
0
51587
TrEMBL
D2TAB7_ERWP6
Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96)
467
0
52090
TrEMBL
C8SYE4_KLEPR
455
0
51028
TrEMBL
A0A1B7I4D9_9ENTR
455
0
50880
TrEMBL
Q3JVE4_BURP1
Burkholderia pseudomallei (strain 1710b)
463
0
50158
TrEMBL
A0A0E1CGC0_KLEPN
465
0
52084
TrEMBL
F6CZH2_MARPP
Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181)
477
0
53838
TrEMBL
B7LV52_ESCF3
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
470
0
52669
TrEMBL
Q63WQ2_BURPS
Burkholderia pseudomallei (strain K96243)
480
0
52115
TrEMBL
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
4 * 28500, calculated, 4 * 28000, SDS-PAGE; native aArDH, 2 * 28500, SDS-PAGE; recombinant aArDH, 2 * 28500, SDS-PAGE
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.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression vector containing the ORF of aArDH under the control of T7 promoter, pET21aArDH, transformed into Escherichia coli strain BL21(DE3)
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
Select items on the left to see more content.
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.
Information
