Any feedback?
No. of entries
Information on EC 1.1.1.427 - D-arabinose 1-dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.427
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
showSynonyms
ara1p, adh-4, nadp(+)-dependent d-arabinose dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adh-4
-
-
-
-
ARA
ARA1
Ara1p
AraDH
D-arabinose dehydrogenase
NADP(+)-dependent D-arabinose dehydrogenase
Sso1300
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinofuranose + NADP+ = D-arabinono-1,4-lactone + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-arabinose degradation III, D-arabinose degradation IV, dehydro-D-arabinono-1,4-lactone biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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: -
Products: -
?
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
ir
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
Substrates: -
Products: -
Products: -
?
acetoin + NADP+
diacetyl + NADPH + H+
-
Substrates: this back reaction only occurs at alkaline pH values (9.0-10.0)
Products: -
Products: -
r
acetoin + NADP+
diacetyl + NADPH + H+
-
Substrates: this back reaction only occurs at alkaline pH values (9.0-10.0)
Products: -
Products: -
r
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + 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: -
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: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-ribose + NADP+
D-ribonolactone + NADPH
Substrates: -
Products: -
Products: -
?
D-ribose + NADP+
D-ribonolactone + NADPH
Substrates: -
Products: -
Products: -
?
diacetyl + NADPH + H+
acetoin + NADP+
-
Substrates: -
Products: -
Products: -
r
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: most active with L-fucose as substrate
Products: -
Products: -
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: most active with L-fucose as substrate
Products: -
Products: -
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
-
Substrates: with NADP+
Products: -
Products: -
?
L-galactose + NADP+
L-galactonolactone + NADPH
Substrates: -
Products: -
Products: -
?
L-galactose + NADP+
L-galactonolactone + NADPH
Substrates: -
Products: -
Products: -
?
L-xylose + NADP+
?
-
Substrates: preferred substrate
Products: -
Products: -
?
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: -
Products: -
?
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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant subunit ARA1p shows 0.5% activity with NAD+ compared to NADPH and has no activity with glycerol
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 Km-value for NAD+ is 30fold higher compared to the Km-value for NADP+
NADP+
the catalytic efficiency of NADP+ in combination with D-arabinose is 36-fold higher than that of NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
NADPH inhibits the enzyme activity competitively with respect to NADP+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.038
NADP+
pH 7.5, 70°C, determined with 10 mM D-arabinose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 100
70°C: about 40% of maximal activity, 100°C: about 90% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). ARADH_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
349
0
37879
Swiss-Prot
-
ARA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
344
0
38884
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
homodimer
homotetramer
monomer
tetramer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose A-50, Sephacryl S-200, Cibacron blue and phenyl-Sepharose CL-4B chromatographies
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.T.; Huh, W.K.; Kim, J.Y.; Hwang, S.W.; Kang, S.O.
D-Arabinose dehydrogenase and biosynthesis of erythroascorbic acid in Candida albicans
Biochim. Biophys. Acta
1297
1-8
1996
Candida albicans, Candida albicans ATCC 10231
brenda
Kim, S.T.; Huh, W.K.; Lee, B.H.; Kang, S.O.
D-Arabinose dehydrogenase and its gene from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
Saccharomyces cerevisiae
brenda
Brouns, S.J.; Turnbull, A.P.; Willemen, H.L.; Akerboom, J.; van der Oost, J.
Crystal structure and biochemical properties of the D-arabinose dehydrogenase from Sulfolobus solfataricus
J. Mol. Biol.
371
1249-1260
2007
Saccharolobus solfataricus (Q97YM2), Saccharolobus solfataricus P2 (Q97YM2)
brenda
Gonzalez, E.; Fernandez, M.R.; Marco, D.; Calam, E.; Sumoy, L.; Pares, X.; Dequin, S.; Biosca, J.A.
Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol
Appl. Environ. Microbiol.
76
670-679
2010
Saccharomyces cerevisiae
brenda
Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment
J. Biol. Chem.
281
27378-27388
2006
Saccharolobus solfataricus (Q97YM2), Saccharolobus solfataricus P2 (Q97YM2)
brenda
Hu, X.Q.; Guo, P.C.; Ma, J.D.; Li, W.F.
Structures of Saccharomyces cerevisiae D-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition
Acta Crystallogr. Sect. F
69
1190-1195
2013
Saccharomyces cerevisiae (P38115)
brenda
van Bergen, B.; Strasser, R.; Cyr, N.; Sheppard, J.D.; Jardim, A.
alpha,beta-Dicarbonyl reduction by Saccharomyces D-arabinose dehydrogenase
Biochim. Biophys. Acta
1760
1636-1645
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda
Amako, K.; Fujita, K.; Iwamoto, C.; Sengee, M.; Fuchigami, K.; Fukumoto, J.; Ogishi, Y.; Kishimoto, R.; Goda, K.
NADP(+)-dependent D-arabinose dehydrogenase shows a limited contribution to erythroascorbic acid biosynthesis and oxidative stress resistance in Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
70
3004-3012
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH250
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.427)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
