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Information on EC 1.1.1.116 - D-arabinose 1-dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.116
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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
1.1.1.116 D-arabinose 1-dehydrogenase (NAD+)
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.116
- l-galactose
- nadp+
- l-fucose
-
d-erythroascorbic
- d-arabinono-1,4-lactone
-
nadp+-dependent
-
five-carbon
- l-ascorbate
- dehydratase
-
sulfolobus
- acetoin
- 2-oxoglutarate
- archaea
- solfataricus
-
sephacryl
- l-xylose
- synthesis
showSynonyms
d-arabinose dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARA
ARA1
Ara2p
arabinose(fucose)dehydrogenase
-
-
-
-
D-arabinose dehydrogenase
dehydrogenase, D-arabinose
-
-
-
-
NAD(+)-specific D-arabinose dehydrogenase
NAD-pentose-dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinose + NAD+ = D-arabinono-1,4-lactone + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
dehydro-D-arabinono-1,4-lactone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
D-arabinose:NAD+ 1-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-47-8
-
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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
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-fucose + NAD+
L-6-deoxyascorbate + NADH
-
Substrates: -
Products: -
Products: -
?
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-ribose + NAD+
2-deoxy-D-ribono-1,4-lactone + NADH
-
Substrates: no substrate for fungal enzyme
Products: -
Products: -
?
2-deoxy-D-ribose + NAD+
2-deoxy-D-ribono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
ir
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the biosynthesis of D-erythroascorbic acid and D-erythroascorbate glucoside from exogeneous D-arabinose in the fungus, overview, D-erythroascorbate is more stable to autoxidation and accumulates in the organism
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: preferred sugar substrate
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: preferred sugar substrate
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: by far the best substrate
Products: -
Products: -
ir, ?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: irreversible reaction at pH 10
Products: -
Products: -
ir, ?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: one of a variety of NAD+ or NADP+ requiring arabinose dehydrogenases, see also 1.1.1.115
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,4-lactone + NADH
-
Substrates: no substrate for bacterial enzyme
Products: -
Products: -
?
D-xylose + NAD+
D-xylono-1,4-lactone + NADH
-
Substrates: poor substrate
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH
-
Substrates: poor substrate
Products: -
Products: -
?
L-fucose + NAD+
L-fuconolactone + NADH
-
Substrates: with NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates for the fungal enzyme are D-fucose, L-xylose, 6-phosphogluconate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates for the bacterial enzyme are D-lyxose, D-fucose, L-rhamnose, 2-deoxy-D-glucose, D-fructose, sucrose, xylitol, L-arabitol, D-arabitol, ribitol, D-sorbitol, D-mannitol, D-galactose, D-mannose
Products: -
Products: -
?
additional information
?
-
Substrates: ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
Products: -
Products: -
?
additional information
?
-
-
Substrates: ARa2p shows a broad sugar substrate specificity, but prefers D-arabinose
Products: -
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
L-fucose + NAD+
L-6-deoxyascorbate + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: the enzyme is involved in the biosynthesis of D-erythroascorbic acid and D-erythroascorbate glucoside from exogeneous D-arabinose in the fungus, overview, D-erythroascorbate is more stable to autoxidation and accumulates in the organism
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: -
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
Substrates: the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
Products: -
Products: -
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
Substrates: one of a variety of NAD+ or NADP+ requiring arabinose dehydrogenases, see also 1.1.1.115
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-arabinose
substrate inhibition of Ara2p at concentrations above 5 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00071
NAD+-dependent Ara2p reaction in presence of 200 mM D-arabinose, native cell extract
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
20% of maximal activity at pH 6.5 and pH 9.0, pH profile
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ARA2; gene YMR041c or ARA2, isozyme Ara2p
SwissProt
brenda
recombinant enzyme overexpressed in Saccharomyces cerevisiae and Zygosaccharomyces bailii
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
ARA1 can only be detected in yeast peptone dextrose 2-DE gel images, thus higher reductive efficiency and higher cofactor availability are obtained with the alternation of cultivation condition (mainly growth medium)
brenda
additional information
-
ARA1 can only be detected in yeast peptone dextrose 2-DE gel images, thus higher reductive efficiency and higher cofactor availability are obtained with the alternation of cultivation condition (mainly growth medium)
-
brenda
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.
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). ARA2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
335
0
38220
Swiss-Prot
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
42000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
ARA2 gene disruption leads to complete loss of NAD+-specific D-arabinose dehydrogenase activity
additional information
-
ARA2 gene disruption leads to complete loss of NAD+-specific D-arabinose dehydrogenase activity
additional information
-
ARA2 gene disruption leads to complete loss of NAD+-specific D-arabinose dehydrogenase activity
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
recombinant His6-tagged Ara2p from Escherichia coli by anion exchange and nickel affinity chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ARA1, co-overexpression of the enzyme and the D-arabinono-1,4-lactone oxidase and/or L-galactono-1,4-lactone dehydrogenase in Saccharomyces cerevisiae strains result in overproduction and accumulation of vitamin C in the culture medium, while overexpression of the D-arabinose dehydrogenase alone does not alter the L-ascorbate content, overview
-
gene YMR041c or ARA2, phylogenetic tree, expression of His6-tagged Ara2p in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
production of L-ascorbic acid and secretion into culture medium by overexpression of enzyme and arabinone-1,4-lactone oxidase in Saccharomyces cerevisiae and Zygosaccharomyces bailii
synthesis
-
production of L-ascorbic acid and secretion into culture medium by overexpression of enzyme and arabinone-1,4-lactone oxidase in Saccharomyces cerevisiae and Zygosaccharomyces bailii
-
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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
brenda
Schiwara, H.W.; Domschke, W.; Domagk, G.F.
Differenzierung verschiedener Zucker-Dehydrogenasen in der Schweineleber durch Disk-Elektrophorese und Ionenaustauschchromatograpie
Hoppe-Seyler's Z. Physiol. Chem.
349
1575-1581
1968
Sus scrofa
brenda
Pincheira G.; Leon G.; Ureta, T.
Aldosugar dehydrogenases from Neurospora crassa. Partial purification and characterization of D-arabinose:NAD dehydrogenase
FEBS Lett.
30
111-114
1973
Neurospora crassa
brenda
Maijub, A.G.; Pecht, M.A.; Miller, G.R.; Carper, W.R.
Arabinose (fucose) dehydrogenase from pig liver. I. Isolation and characterization
Biochim. Biophys. Acta
315
37-42
1973
Sus scrofa
brenda
Carper, W.R.; Chang, K.W.; Thorpe, W.G.; Carper, M.A.; Buess, C.M.
Arabinose (fucose) dehydrogenase from pig liver. II. Steady-state kinetics
Biochim. Biophys. Acta
358
49-56
1974
Sus scrofa
brenda
Carrasco, A.; Pincheira, G.; Ureta, T.
Genetic and biochemical characterization of D-arabinose dehydrogenase from Neurospora crassa
J. Bacteriol.
145
164-170
1981
Neurospora crassa
brenda
Yamanaka, K.
Specific microassay of D-arabinose and L-fucose with D-arabinose (L-fucose) dehydrogenase
Agric. Biol. Chem.
39
2227-2234
1975
Pseudomonas sp.
-
brenda
Sauer, M.; Branduardi, P.; Valli, M.; Porro, D.
Production of L-ascorbic acid by metabolically engineered Saccharomyces cerevisiae and Zygosaccharomyces bailii
Appl. Environ. Microbiol.
70
6086-6091
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae GRF18U
brenda
Amako, K.; Fujita, K.; Shimohata, T.A.; Hasegawa, E.; Kishimoto, R.; Goda, K.
NAD(+)-specific D-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae
FEBS Lett.
580
6428-6434
2006
Saccharomyces cerevisiae (Q04212), Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH250 (Q04212)
brenda
Baroja-Mazo, A.; del Valle, P.; Rua, J.; de Cima, S.; Busto, F.; de Arriaga, D.; Smirnoff, N.
Characterisation and biosynthesis of D-erythroascorbic acid in Phycomyces blakesleeanus
Fungal Genet. Biol.
42
390-402
2005
Phycomyces blakesleeanus
brenda
Lin, J.; Liu, Q.; Su, E.; Wei, D.; Yang, S.
Application of comparative proteome analysis to reveal influence of cultivation conditions on asymmetric bioreduction of beta-keto ester by Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
80
831-839
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae LH1
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.116)
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