Information on EC 1.1.1.250 - D-arabinitol 2-dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.1.250
-
RECOMMENDED NAME
GeneOntology No.
D-arabinitol 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-arabinitol + NAD+ = D-ribulose + NADH + H+
show the reaction diagram
in the reverse reaction the enzyme catalyzes transfer of 4(S) hydrogen of NADH
-
D-arabinitol + NAD+ = D-ribulose + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Pentose and glucuronate interconversions
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
arabitol 2-dehydrogenase
-
-
ArDH
-
-
-
-
D-arabinitol 2-dehydrogenase (ribulose-forming)
-
-
-
-
D-arabinitol dehydrogenase
-
-
-
-
dehydrogenase, D-arabinitol (Candida albicans clone pEMBLYe23 gene arDH reduced)
-
-
-
-
NAD-dependent arabitol dehydrogenase (Candida albicans clone pEMBLYe23)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
336883-93-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene tm0297
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
-
-
-
-
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
-
-
-
-
r
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
-
r
-
-
D-arabinitol + NAD+
D-ribulose + NADH + H+
show the reaction diagram
Candida albicans B331
-
-
-
-
D-ribulose + NADH
D-arabinitol + NAD+
show the reaction diagram
Candida albicans, Candida albicans B331
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
-
D-xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
r
D-xylulose + NADH
?
show the reaction diagram
-
1% of the activity with D-ribulose
-
-
-
Galactitol + NAD+
?
show the reaction diagram
-
1.6% of the activity with D-arabinitol
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
5% of the activity with D-arabinitol
-
-
-
L-Xylulose + NADH
?
show the reaction diagram
-
3% of the activity with D-ribulose
-
-
-
additional information
?
-
-
the enzyme exclusively catalyzed the NAD(H)-dependent oxidoreduction of D-arabitol, D-xylitol, D-ribulose, or D-xylulose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-ribulose + NADH
D-arabinitol + NAD+
show the reaction diagram
Candida albicans, Candida albicans B331
-
catalyzes the final step in the synthesis of D-arabinitol
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
dependent on
NADH
-
dependent on
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
twofold activation at 60 mM, contributes to the overall stability of the protein and ise 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+
-
1-5 mM, 50% increase of activity
additional information
-
no effect on the activity by CaCl2 or NaCl
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.6
-
D-Arabinitol
-
pH 8.5, 85C, recombinant detagged enzyme
7.1
-
D-Arabinitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
39.8
-
D-Arabinitol
-
-
7.2
-
D-ribulose
-
pH 7.5, 85C, recombinant detagged enzyme
13.9
-
D-ribulose
-
pH 7.5, 85C, recombinant Strep-tagged enzyme
20
-
D-xylitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
21.7
-
D-xylitol
-
pH 8.5, 85C, recombinant detagged enzyme
0.059
-
NAD+
-
with D-arabinitol, pH 8.5, 85C, recombinant detagged enzyme
0.069
-
NAD+
-
with D-arabinitol, pH 8.5, 85C, recombinant Strep-tagged enzyme
0.12
-
NAD+
-
-
0.027
-
NADH
-
with D-ribulose, pH 7.5, 85C, recombinant Strep-tagged enzyme
0.031
-
NADH
-
with D-ribulose, pH 7.5, 85C, recombinant detagged enzyme
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11
-
D-Arabinitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
18.7
-
D-Arabinitol
-
pH 8.5, 85C, recombinant detagged enzyme
165.6
-
D-ribulose
-
pH 7.5, 85C, recombinant Strep-tagged enzyme
193.2
-
D-ribulose
-
pH 7.5, 85C, recombinant detagged enzyme
11.2
-
D-xylitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
16.6
-
D-xylitol
-
pH 8.5, 85C, recombinant detagged enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
D-Arabinitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
9091
7.2
-
D-Arabinitol
-
pH 8.5, 85C, recombinant detagged enzyme
9091
12
-
D-ribulose
-
pH 7.5, 85C, recombinant Strep-tagged enzyme
9353
27
-
D-ribulose
-
pH 7.5, 85C, recombinant detagged enzyme
9353
0.56
-
D-xylitol
-
pH 8.5, 85C, recombinant Strep-tagged enzyme
9397
0.74
-
D-xylitol
-
pH 8.5, 85C, recombinant detagged enzyme
9397
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
reduction reaction
8.5
-
-
oxidation reaction
10
11
-
oxidation of D-arabinitol
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
8
11
-
pH 8.0: about 40% of maximal activity, pH 8.5: about 60% of maximal activity, pH 10-11: maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
85
-
inactive below 50C, optimal activity at 85C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
Thermotoga maritima cannot use D-arabitol as a sole carbon source. Optimal growth temperature of Thermotoga maritima is 80C
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
164000
-
-
native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 31000, SDS-PAGE
homohexamer
-
6 * 27600, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
11
-
-
unstable above
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
85
-
-
rapid inactivation of the recombinant Strep-tagged enzyme, while the detagged enzyme retains over 90% activity after 90 min at 85C
additional information
-
-
the addition of the Strep-tag led to a destabilization of tmArDH resulting in the loss of thermostability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Mg2+ enhances the stability
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli and Saccharomyces cerevisiae
-
gene tm0297, located in an operon with tm0298 encoding a mannitol dehydrogenase, phylogenetic analysis, expression of the Strep-tagged enzyme in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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