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Information on EC 1.1.1.427 - D-arabinose 1-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.427
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.427 D-arabinose 1-dehydrogenase (NADP+)
IUBMB Comments
The enzyme from the archaeon Saccharolobus solfataricus is tetrameric and contains zinc. L-fucose also is a substrate. In contrast to EC 1.1.1.116 (D-arabinose 1-dehydrogenase (NAD+)) and EC 1.1.1.117 (D-arabinose 1-dehydrogenase [NAD(P)+]), this enzyme is specific for NADP+.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
showD-arabinofuranose
+
=
+
+
Synonyms
ara1p, adh-4, nadp(+)-dependent d-arabinose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adh-4
-
-
-
-
ARA
ARA1
Ara1p
AraDH
D-arabinose dehydrogenase
NADP(+)-dependent D-arabinose dehydrogenase
Sso1300
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinofuranose + NADP+ = D-arabinono-1,4-lactone + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-arabinose degradation III, D-arabinose degradation IV, dehydro-D-arabinono-1,4-lactone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
D-arabinose:NADP+ 1-oxidoreductase
The enzyme from the archaeon Saccharolobus solfataricus is tetrameric and contains zinc. L-fucose also is a substrate. In contrast to EC 1.1.1.116 (D-arabinose 1-dehydrogenase (NAD+)) and EC 1.1.1.117 (D-arabinose 1-dehydrogenase [NAD(P)+]), this enzyme is specific for NADP+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R/S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + NADP+
-
Substrates: 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
Products: -
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?
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
-
Substrates: -
Products: -
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?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
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ir
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: -
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?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
Substrates: -
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?
L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
-
Substrates: -
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?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
-
Substrates: -
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?
L-galactose + NADP+
L-galactonolactone + NADPH
Substrates: -
Products: -
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?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
-
Substrates: -
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?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
Substrates: -
Products: -
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?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
Substrates: -
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?
acetoin + NADP+
diacetyl + NADPH + H+
-
Substrates: this back reaction only occurs at alkaline pH values (9.0-10.0)
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r
acetoin + NADP+
diacetyl + NADPH + H+
-
Substrates: this back reaction only occurs at alkaline pH values (9.0-10.0)
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r
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
Substrates: -
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?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
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?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
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?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
Products: -
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?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
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?
D-ribose + NADP+
D-ribonolactone + NADPH
Substrates: -
Products: -
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?
D-ribose + NADP+
D-ribonolactone + NADPH
Substrates: -
Products: -
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?
diacetyl + NADPH + H+
acetoin + NADP+
-
Substrates: -
Products: -
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r
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: -
Products: -
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?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: most active with L-fucose as substrate
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?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: -
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?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: most active with L-fucose as substrate
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?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
-
Substrates: with NADP+
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?
additional information
?
-
Substrates: the enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. Negligible activity with D-glucose, D-galactose, D-fucose, L-arabinose and D-xylose
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?
additional information
?
-
Substrates: the enzyme is specific for sugars with D-arabinose-type hydroxyl group stereo-configurations at C3 and C4. Negligible activity with D-glucose, D-galactose, D-fucose, L-arabinose and D-xylose
Products: -
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?
additional information
?
-
-
Substrates: 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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?
additional information
?
-
-
Substrates: the recombinant subunit ARA1p shows 0.5% activity with NAD+ compared to NADPH and has no activity with glycerol
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additional information
?
-
-
Substrates: the recombinant subunit ARA1p shows 0.5% activity with NAD+ compared to NADPH and has no activity with glycerol
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
Substrates: the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the catalytic efficiency of NADP+ in combination with D-arabinose is 36-fold higher than that of NAD+
NADP+
the catalytic efficiency of NADP+ in combination with D-arabinose is 36-fold higher than that of NAD+
NADP+
the Km-value for NAD+ is 30fold higher compared to the Km-value for NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
contains two endogenous zinc ions per subunit.A zinc ion is bound in the loop that protrudes from the catalytic domain. This zinc is tetrahedrally coordinated by residues D94, C97, C100 and C108
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
NADPH inhibits the enzyme activity competitively with respect to NADP+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.038
NADP+
pH 7.5, 70°C, determined with 10 mM D-arabinose
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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
10.6
D-arabinose
pH 7.5, 70°C, determined with 0.4 mM NADP+
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IC50 VALUE [mM]
INHIBITOR
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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1 - 9.1
pH 7.1: about 40% of maximal activity, pH 9.1: about 60% of maximal activity, pH 9.5: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 100
70°C: about 40% of maximal activity, 100°C: about 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
-
an enzyme-deficient mutant shows increased susceptibility to H2O2 and diamide but not to menadione or tert-butylhydroperoxide
malfunction
-
enzyme knockout mutants exhibit a decreased growth rate phenotype in media containing diacetyl
malfunction
-
enzyme knockout mutants exhibit a decreased growth rate phenotype in media containing diacetyl
-
malfunction
-
an enzyme-deficient mutant shows increased susceptibility to H2O2 and diamide but not to menadione or tert-butylhydroperoxide
-
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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). ARA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
344
0
38884
Swiss-Prot
-
Q97YM2_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
349
0
37879
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homodimer
homotetramer
monomer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structure is solved to a resolution of 1.80 A by single-wavelength anomalous diffraction and phased using the two endogenous zinc ions per subunit. The structure reveals a catalytic and cofactor binding domain
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
-
the enzyme is relatively stable from pH 4.5 to 7.5 after 24 h incubation
764189
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 50
-
the enzyme loses 50% of its activity at 35°C for 60 min and is completely inactivated at 50°C in 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged storage at 4°C, freezing and thawing, and lyophilisation of enzyme solutions result in significant losses of the enzyme activity
-