Information on EC 1.1.1.301 - D-arabitol-phosphate dehydrogenase

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The expected taxonomic range for this enzyme is: Enterococcus avium

EC NUMBER
COMMENTARY hide
1.1.1.301
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RECOMMENDED NAME
GeneOntology No.
D-arabitol-phosphate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabitol 1-phosphate + NAD+ = D-xylulose 5-phosphate + NADH + H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
D-arabitol-phosphate:NAD+ oxidoreductase
This enzyme participates in arabitol catabolism. The enzyme also converts D-arabitol 5-phosphate to D-ribulose 5-phosphate at a lower rate [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabitol 1-phosphate + NAD+
D-xylulose 5-phosphate + NADH + H+
show the reaction diagram
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r
D-arabitol 1-phosphate + NADP+
D-xylulose 5-phosphate + NADPH + H+
show the reaction diagram
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r
D-arabitol 5-phosphate + NAD+
D-ribulose 5-phosphate + NADH + H+
show the reaction diagram
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-
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?
D-arabitol 5-phosphate + NADP+
D-ribulose 5-phosphate + NADPH + H+
show the reaction diagram
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?
xylulose 5-phosphate + NADH
D-arabitol 1-phosphate + NAD+
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH
NADP+
the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH
NADPH
the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
required. Pure APDH contains 4.05 ions of Mn2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
xylulose 5-phosphate does not protect the enzyme from EDTA inactivation. Addition of Mn2+ at concentrations of up to 2 mM results in complete reactivation of APDH
Hg2+
2 mM, complete inactivation
PHMB
2 mM, complete inactivation
Zn2+
2 mM, complete inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 3.6
D-arabitol 1-phosphate
0.63
D-arabitol 5-phosphate
20°C, pH 8.5, cofactor: NAD+
0.23 - 0.65
D-xylulose 5-phosphate
0.71 - 0.8
NAD+
0.021
NADH
20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate
2.7
NADP+
20°C, pH 8.5, cosubstrate: D-arabitol 1-phosphate
0.24
NADPH
20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.4
reduction of D-xylulose 5-phosphate with NADH or NADPH
8.3 - 8.6
oxidation of D-arabitol 1-phosphate with NAD+ or NADP+
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
4 * 41000, SDS-PAGE
160000
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 41000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Bacillus subtilis. Expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain results in a strain of Bacillus subtilis capable of converting D-glucose to D-arabitol with a high yield (28%) and little by-product formation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain results in a strain of Bacillus subtilis capable of converting D-glucose to D-arabitol with a high yield (28%) and little by-product formation
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