Information on EC 1.1.1.117 - D-arabinose 1-dehydrogenase [NAD(P)+]

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

EC NUMBER
COMMENTARY hide
1.1.1.117
-
RECOMMENDED NAME
GeneOntology No.
D-arabinose 1-dehydrogenase [NAD(P)+]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dehydro-D-arabinono-1,4-lactone biosynthesis
-
-
degradation of pentoses
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-
SYSTEMATIC NAME
IUBMB Comments
D-arabinose:NAD(P)+ 1-oxidoreductase
Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-48-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
a double mutant DELATbdh1 and DELTA ara1 strain still produces (2S,3S)-2,3-butanediol and meso-2,3-butanediol suggesting only a minor role of Ara1p in the production of 2,3-butanediol
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R/S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + NADP+
show the reaction diagram
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Ara1p is as an oxidoreductase that can reduce racemic acetoin to meso-2,3-butanediol and (2S,3S)-2,3-butanediol in the presence of NADPH
-
-
?
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
show the reaction diagram
L-colitose + NAD(P)+
3,6-dideoxy-L-galactono-1,5-lactone + NAD(P)H
show the reaction diagram
-
i.e. 3,6-dideoxy-L-galactose
-
?
L-fucose + NAD(P)+
6-deoxy-L-galactono-1,4-lactone + NAD(P)H
show the reaction diagram
L-galactose + NAD(P)+
L-galactono-1,4-lactone + NAD(P)H
show the reaction diagram
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
show the reaction diagram
additional information
?
-
-
enzyme in addition acts as a NADPH-dependent oxidoreductase producing meso-2,3-butanediol and (2S,3S)-2,3-butanediol from (R,S)-acetoin
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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
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
competitive to NADP+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82 - 161
D-arabinose
28.9 - 98
L-fucose
91.3 - 180
L-galactose
24 - 37.1
L-Xylose
22
NAD+
-
-
0.000061 - 2.3
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0786
NADPH
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.2
-
about 80% of maximal activity at pH 7.3 and 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
24
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
gel filtration
50000
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gel filtration
74000
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gel filtration
104000
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sedimentation analysis in EDTA/phosphate buffer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
1 * 40000 + 1 + 39000, SDS-PAGE
monomer
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1 * 42000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
after 10 min 90% of maximal activity retained
58
-
half-life of 20 s is increased to 80 s in presence of cofactor, in both cases biphasic inactivation curve
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, acetone-dried cells retain full activity for extended periods of time
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4°C, stable as ammonium sulfate precipitate
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frozen, purified enzyme stable for many months
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lyophilized, purified enzyme stable for many months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial; using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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