We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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
Synonyms
adh-4 , ara1p, nadp(+)-dependent d-arabinose dehydrogenase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-arabinose dehydrogenase
NADP(+)-dependent D-arabinose dehydrogenase
ARA
-
-
ARA1
-
-
Ara1p
-
-
AraDH
-
D-arabinose dehydrogenase
-
-
D-arabinose dehydrogenase
-
-
-
D-arabinose dehydrogenase
-
-
D-arabinose dehydrogenase
-
-
-
NADP(+)-dependent 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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
(R/S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + NADP+
-
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
-
-
?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
acetoin + NADP+
diacetyl + NADPH + H+
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
-
-
-
-
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
-
-
-
ir
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
D-ribose + NADP+
D-ribonolactone + NADPH
D-xylose + NADP+
D-xylonolactone + NADPH + H+
-
-
-
-
?
diacetyl + NADPH + H+
acetoin + NADP+
L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
-
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
L-galactose + NADP+
L-galactono-1,5-lactone + NADPH + H+
-
-
-
-
?
L-galactose + NADP+
L-galactonolactone + NADPH
-
-
-
?
L-gulose + NADP+
?
-
-
-
-
?
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
-
-
-
-
?
methylglyoxal + NADPH + H+
?
additional information
?
-
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
-
-
-
?
2,3-pentanedione + NADPH + H+
hydroxypentanone + NADP+
-
-
-
-
?
acetoin + NADP+
diacetyl + NADPH + H+
-
this back reaction only occurs at alkaline pH values (9.0-10.0)
-
-
r
acetoin + NADP+
diacetyl + NADPH + H+
-
this back reaction only occurs at alkaline pH values (9.0-10.0)
-
-
r
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
-
-
-
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH + H+
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-1actone + NADPH + H+
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-lyxose + NADP+
?
-
-
-
-
?
D-lyxose + NADP+
?
-
-
-
-
?
D-ribose + NADP+
D-ribonolactone + NADPH
-
-
-
?
D-ribose + NADP+
D-ribonolactone + NADPH
-
-
-
?
diacetyl + NADPH + H+
acetoin + NADP+
-
-
-
-
r
diacetyl + NADPH + H+
acetoin + NADP+
-
-
-
-
r
L-fucose + NADP+
?
-
-
-
-
?
L-fucose + NADP+
?
-
-
-
-
?
L-fucose + NADP+
?
-
-
-
-
?
L-fucose + NADP+
?
-
-
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
-
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
most active with L-fucose as substrate
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
-
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
most active with L-fucose as substrate
-
-
?
L-fucose + NADP+
L-fuconolactone + NADPH + H+
-
with NADP+
-
-
?
L-galactose + NADP+
?
-
-
-
-
?
L-galactose + NADP+
?
-
-
-
-
?
L-galactose + NADP+
?
-
-
-
-
?
L-galactose + NADP+
?
-
-
-
-
?
L-xylose + NADP+
?
-
-
-
-
?
L-xylose + NADP+
?
-
-
-
-
?
L-xylose + NADP+
?
-
preferred substrate
-
-
?
methylglyoxal + NADPH + H+
?
-
-
-
-
?
methylglyoxal + NADPH + H+
?
-
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
additional information
?
-
-
the recombinant subunit ARA1p shows 0.5% activity with NAD+ compared to NADPH and has no activity with glycerol
-
-
-
additional information
?
-
-
the recombinant subunit ARA1p shows 0.5% activity with NAD+ compared to NADPH and has no activity with glycerol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
-
-
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+
the catalytic efficiency of NADP+ in combination with D-arabinose is 36-fold higher than that of NAD+
NADP+
-
-
NADP+
-
preferred cofactor
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+
NADPH
-
NADPH
-
the enzyme specifically utilizes NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
not influenced by Ca2+
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
Zn2+
contains two zinc ions per monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-chloromercuribenzoic acid
-
75% residual activity at 1 mM
Cu2+
-
69% residual activity at 1 mM
Fe2+
-
37% residual activity at 1 mM
Hg2+
-
complete inhibition at 1 mM
Mg2+
-
85% residual activity at 1 mM
Mn2+
-
87% residual activity at 1 mM
N-ethylmaleimide
-
54% residual activity at 1 mM
NADPH
-
NADPH inhibits the enzyme activity competitively with respect to NADP+
Zn2+
-
48% residual activity at 1 mM
additional information
-
not inhibited by EDTA and dithiothreitol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.2
2,3-Pentanedione
-
at pH 7.0 and 25°C
160
D-Lyxose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
7.7
diacetyl
-
at pH 7.0 and 25°C
210
L-gulose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
14.3
methylglyoxal
-
at pH 7.0 and 25°C
1.25
NAD+
pH 7.5, 70°C, determined with 10 mM D-arabinose
0.014
NADPH
-
at pH 7.0 and 25°C
1.4
D-arabinose
pH 7.5, 70°C, determined with 0.4 mM NADP+
29.2
D-arabinose
-
at pH 8.0 and 30°C
220
D-arabinose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
0.22
L-fucose
pH 7.5, 70°C, determined with 0.4 mM NADP+
28.9
L-fucose
-
at pH 8.0 and 30°C
310
L-fucose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
91.3
L-galactose
-
at pH 8.0 and 30°C
330
L-galactose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
24
L-Xylose
-
-
37.1
L-Xylose
-
at pH 8.0 and 30°C
110
L-Xylose
-
recombinant subunit ARA1p, at pH 8.2 and 25°C
0.038
NADP+
pH 7.5, 70°C, determined with 10 mM D-arabinose
0.0446
NADP+
-
with D-arabinose as cosubstrate, at pH 8.0 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.9
2,3-Pentanedione
-
at pH 7.0 and 25°C
17.7
D-ribose
pH 7.5, 80°C
6.9
diacetyl
-
at pH 7.0 and 25°C
63.4
L-Xylose
-
at pH 8.0 and 30°C
4.4
methylglyoxal
-
at pH 7.0 and 25°C
3.7
NADPH
-
at pH 7.0 and 25°C
23.8
D-arabinose
pH 7.5, 80°C
68.2
D-arabinose
-
at pH 8.0 and 30°C
26.8
L-fucose
pH 7.5, 80°C
69.5
L-fucose
-
at pH 8.0 and 30°C
17.7
L-galactose
pH 7.5, 80°C
53.2
L-galactose
-
at pH 8.0 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.41
2,3-Pentanedione
-
at pH 7.0 and 25°C
0.9
diacetyl
-
at pH 7.0 and 25°C
0.58
L-galactose
-
at pH 8.0 and 30°C
1.71
L-Xylose
-
at pH 8.0 and 30°C
0.3
methylglyoxal
-
at pH 7.0 and 25°C
14.5
NAD+
pH 7.5, 70°C, determined with 10 mM D-arabinose
525
NADP+
pH 7.5, 70°C, determined with 10 mM D-arabinose
257
NADPH
-
at pH 7.0 and 25°C
2.34
D-arabinose
-
at pH 8.0 and 30°C
10.6
D-arabinose
pH 7.5, 70°C, determined with 0.4 mM NADP+
2.4
L-fucose
-
at pH 8.0 and 30°C
67
L-fucose
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.
0.0786
NADPH
Candida albicans
-
at pH 8.0 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 5
-
pH optimum for the diacetyl reduction reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
7.3 - 9.3
more than 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70 - 100
70°C: about 40% of maximal activity, 100°C: about 90% of maximal activity
74 - 100
more than 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37291
4 * 37291, calculated from sequence
39000
-
1 * 39000 + 1 * 40000, SDS-PAGE
72000 - 75000
-
gel filtration
75000 - 80000
-
gel filtration
40000
-
1 * 39000 + 1 * 40000, SDS-PAGE
40000
-
1 * 40000 + 1 + 39000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
1 * 39000 + 1 * 40000, SDS-PAGE
heterodimer
-
1 * 40000 + 1 + 39000, SDS-PAGE
heterodimer
-
1 * 40000 + 1 * 39000, SDS-PAGE
heterodimer
-
1 * 40000 + 1 * 39000, SDS-PAGE
-
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 40000, SDS-PAGE
-
homotetramer
-
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
-
tetramer
4 * 37291, calculated from sequence
tetramer
-
4 * 37291, calculated from sequence
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
crystal structure at 2 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5 - 7.5
-
the enzyme is relatively stable from pH 4.5 to 7.5 after 24 h incubation
764189
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
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.
-20°C, 20% (v/v) glycerol, at least 2 months, no loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate precipitation, DEAE-Sepharose A-50, Sephacryl S-200, Cibacron blue and phenyl-Sepharose CL-4B chromatographies
-
Ni-NTA column chromatography
-
using Ni-NTA chromatography
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli ER2566 cells
-
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
Select items on the left to see more content.
html completed