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Information on EC 1.1.1.250 - D-arabinitol 2-dehydrogenase
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1.1.1.250 D-arabinitol 2-dehydrogenaseSpecify your search results
Word Map
- 1.1.1.250
-
candidiasis
- candida
- xylitol
- dehydrogenases
- polyols
- ribitol
- albicans
- l-arabinitol
-
roche
-
polyhydric
-
klebsiella
- d-mannitol
-
fluorometric
- stipitis
-
pichia
- tropicalis
- d-fructose
- d-xylulose
-
cobas
-
diagnose
-
nad-dependent
- pentitol
- pneumoniae
- galactitol
- synthesis
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
d-arabinitol dehydrogenase, arabitol 2-dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ArDH
D-arabinitol 2-dehydrogenase (ribulose-forming)
-
-
-
-
D-arabinitol dehydrogenase
-
-
-
-
D-arabitol 2-dehydrogenase
dehydrogenase, D-arabinitol (Candida albicans clone pEMBLYe23 gene arDH reduced)
-
-
-
-
NAD-dependent arabitol dehydrogenase (Candida albicans clone pEMBLYe23)
-
-
-
-
TM_0297
ArDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NAD+ = D-ribulose + NADH + H+
in the reverse reaction the enzyme catalyzes transfer of 4(S) hydrogen of NADH
-
D-arabinitol + NAD+ = D-ribulose + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming)
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CAS REGISTRY NUMBER
COMMENTARY
336883-93-3
-
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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
additional information
?
-
-
the enzyme exclusively catalyzed the NAD(H)-dependent oxidoreduction of D-arabitol, D-xylitol, D-ribulose, or D-xylulose
-
-
?
D-ribulose + NADH
D-arabinitol + NAD+
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
?
D-ribulose + NADH
D-arabinitol + NAD+
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
?
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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
D-ribulose + NADH
D-arabinitol + NAD+
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
?
D-ribulose + NADH
D-arabinitol + NAD+
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
additional information
K+
-
twofold activation at 60 mM, contributes to the overall stability of the protein and ise not required for catalytic activity
K+
60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity
Mg2+
-
twofold activation at 55 mM, contributes to the overall stability of the protein and is not required for catalytic activity
Mg2+
55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity
additional information
no effect on the activity is observed with CaCl2 or NaCl addition, up to 150 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.059
NAD+
-
with D-arabinitol, pH 8.5, 85°C, recombinant detagged enzyme
0.069
NAD+
-
with D-arabinitol, pH 8.5, 85°C, recombinant Strep-tagged enzyme
0.069
NAD+
85°C, pH 8.5, Strep-tagged enzyme, cosubstrate D-arabitol
0.027
NADH
-
with D-ribulose, pH 7.5, 85°C, recombinant Strep-tagged enzyme
0.027
NADH
85°C, pH 7.5, Strep-tagged enzyme, cosubstrate D-ribulose
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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
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
5.5 - 8.5
pH 5.5: about 40% of maximal activity, pH 8.5: about 10% of maximal activity, reduction of D-ribulose
8 - 11
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pH 8.0: about 40% of maximal activity, pH 8.5: about 60% of maximal activity, pH 10-11: maximal activity
4.5 - 9.5
-
40% and 10% of maximal activity at pH 5.5 and pH 8.5, no activity below pH 4.5 and above pH 9.5
4.5 - 9.5
oxidation of D-arabitol is not observed below pH 4.5 or above pH 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
Thermotoga maritima cannot use D-arabitol as a sole carbon source. Optimal growth temperature of Thermotoga maritima is 80°C
brenda
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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). ARDH_CANAW
Candida albicans (strain WO-1)
281
0
30643
Swiss-Prot
other Location (Reliability: 1)
ARDH_CANTR
282
0
30748
Swiss-Prot
other Location (Reliability: 1)
ARDH_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
278
0
30003
Swiss-Prot
other Location (Reliability: 3)
ALX1_AMBMO
272
0
29636
Swiss-Prot
other Location (Reliability: 3)
A0A8J5EG56_9ASCO
313
0
33213
TrEMBL
other Location (Reliability: 4)
K0KFI8_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
278
0
29977
TrEMBL
other Location (Reliability: 2)
A0A8J5EHR8_9ASCO
341
0
36858
TrEMBL
other Location (Reliability: 5)
W1QLS3_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
274
0
30023
TrEMBL
other Location (Reliability: 2)
A2R5Y5_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
320
0
34828
TrEMBL
Mitochondrion (Reliability: 1)
D7RMR7_9ASCO
282
0
30544
TrEMBL
other Location (Reliability: 3)
A2QIN8_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
297
0
31819
TrEMBL
other Location (Reliability: 2)
B9WIA0_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
281
0
30673
TrEMBL
other Location (Reliability: 1)
A0A0F4YYU2_TALEM
362
0
39005
TrEMBL
Mitochondrion (Reliability: 1)
A0A0F4YT44_TALEM
313
0
34233
TrEMBL
Mitochondrion (Reliability: 3)
Q5E8K3_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
256
0
28038
TrEMBL
-
A0A8J5BUU4_9ASCO
339
0
36693
TrEMBL
other Location (Reliability: 5)
Q6T5L8_EMEND
368
0
39686
TrEMBL
Mitochondrion (Reliability: 2)
C5P544_COCP7
Coccidioides posadasii (strain C735)
382
0
41230
TrEMBL
Mitochondrion (Reliability: 2)
Q9WYD3_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
257
0
27886
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
164000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homododecamer
homohexamer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
additional information
-
the addition of the Strep-tag led to a destabilization of tmArDH resulting in the loss of thermostability
85
-
rapid inactivation of the recombinant Strep-tagged enzyme, while the detagged enzyme retains over 90% activity after 90 min at 85°C
85
the tag-less protein is thermostable, retaining 90% of its activity after 90 min. The Strep-tagged enzyme loese 60% of its activity after 10 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
K+, 60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity
Mg2+, 55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from Escherichia coli with and without a Strep-tag. The tag-less form of D-arabitol dehydrogenase has similar kinetic parameters compared to the tagged enzyme, demonstrating that the Strep-tag is not deleterious to protein function but decreases protein stability
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tm0297, located in an operon with tm0298 encoding a mannitol dehydrogenase, phylogenetic analysis, expression of the Strep-tagged enzyme in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the specificity of the enzyme makes it useful for the development of a simple and specific method for the measurement of D-arabinitol, a metabolite of the pathogenic Candida spp. which has been described as a marker for disseminated candidiasis
synthesis
synthesis
the enzyme catalyzed oxidation of D-arabitol to D-ribulose which is a rare ketopentose sugar that has numerous industrially applications. D-Arabitol 2-dehydrogenase from Thermotoga maritima has the potential to be a useful biocatalyst for the production of D-ribulose starting from the inexpensive D-arabitol due to its regiospecificity and thermostability
synthesis
-
the enzyme catalyzed oxidation of D-arabitol to D-ribulose which is a rare ketopentose sugar that has numerous industrially applications. D-Arabitol 2-dehydrogenase from Thermotoga maritima has the potential to be a useful biocatalyst for the production of D-ribulose starting from the inexpensive D-arabitol due to its regiospecificity and thermostability
-
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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
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
Kallnik, V.; Schulz, C.; Schultz, C.; Schweiger, P.; Deppenmeier, U.
Properties of recombinant Strep-tagged and untagged hyperthermophilic D-arabitol dehydrogenase from Thermotoga maritima
Appl. Microbiol. Biotechnol.
90
1285-1293
2011
Thermotoga maritima
brenda
Kallnik, V.; Schultz, C.; Schweiger, P.; Deppenmeier, U.
Properties of recombinant Strep-tagged and untagged hyperthermophilic D-arabitol dehydrogenase from Thermotoga maritima
Appl. Microbiol. Biotechnol.
90
1285-1293