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Information on EC 1.1.1.117 - D-arabinose 1-dehydrogenase [NAD(P)+] for references in articles please use BRENDA:EC1.1.1.117Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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D-arabinose 1-dehydrogenase [NAD(P)+]
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D-arabinose + NAD(P)+ = D-arabinono-1,4-lactone + NAD(P)H + H+
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dehydro-D-arabinono-1,4-lactone biosynthesis
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degradation of pentoses
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D-arabinose:NAD(P)+ 1-oxidoreductase
Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose.
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D-arabinose dehydrogenase
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dehydrogenase, D-arabinose (nicotinamide adenine dinucleotide (phosphate))
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G6
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G6
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UniProt
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malfunction
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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
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
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L-colitose + NAD(P)+
3,6-dideoxy-L-galactono-1,5-lactone + NAD(P)H
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i.e. 3,6-dideoxy-L-galactose
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L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
L-galactose + NADP+
L-galactono-1,4-lactone + NADPH + H+
L-xylose + NADP+
L-xylono-1,4-lactone + NADPH
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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alpha-anomer preferred
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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specific for sugars of the optical configuration of L-galactose
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
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L-fucose + NADP+
6-deoxy-L-galactono-1,4-lactone + NADPH + H+
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i.e. 6-deoxy-L-galactose
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L-galactose + NADP+
L-galactono-1,4-lactone + NADPH + H+
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L-galactose + NADP+
L-galactono-1,4-lactone + NADPH + H+
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beta-anomer preferred
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH + H+
P38115
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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specific for sugars of the optical configuration of L-galactose
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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D-arabinose + NAD(P)+
D-arabino-1,4-lactone + NAD(P)H
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NAD+
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NADP+ and NAD+ equally effective
NAD+
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the affinity for NADP+ is considerably higher
NADP+
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NADP+
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NADP+ and NAD+ equally effective
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NADPH
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competitive to NADP+
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0.82
D-arabinose
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0.000061
NADP+
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7.3 - 9.2
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about 80% of maximal activity at pH 7.3 and 9.2
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Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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20000
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x * 20000, sedimentation analysis in 4.2 M guanidinium chloride, presence of subunits of unequal size might be possible
42000
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1 * 42000, SDS-PAGE
104000
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sedimentation analysis in EDTA/phosphate buffer
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homodimer
x-ray crystallography
monomer
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1 * 42000, SDS-PAGE
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x * 20000, sedimentation analysis in 4.2 M guanidinium chloride, presence of subunits of unequal size might be possible
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x * 20000, sedimentation analysis in 4.2 M guanidinium chloride, presence of subunits of unequal size might be possible
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apo and NADPH-complexed enzyme forms, hanging drop vapor diffusion method, using 25% (w/v) polyethylene glycol 3350, 0.1 M HEPES pH 7.5
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after 10 min 90% of maximal activity retained
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half-life of 20 s is increased to 80 s in presence of cofactor, in both cases biphasic inactivation curve
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-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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Ni-NTA column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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ARA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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38884
Swiss-Prot
W1Q7N1_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
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35433
TrEMBL
A0A1S7UL89_ROSNE
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37048
TrEMBL
A0A2H3F762_9HELO
388
42672
TrEMBL
A0A0B2PE94_GLYSO
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7584
TrEMBL
A0A084FV16_9PEZI
325
36940
TrEMBL
Q97YM2_SULSO
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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37879
TrEMBL
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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
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Cline, A.L.; Hu, A.S.L.
The isolation of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4488-4492
1965
Pseudomonas sp., Pseudomonas sp. G6
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Cline, A.L.; Hu, A.S.L.
Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4493-4497
1965
Pseudomonas sp., Pseudomonas sp. G6
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Cline, A.L.; Hu, A.S.L.
Some physical properties of three sugar dehydrogenases from a pseudomonad
J. Biol. Chem.
240
4498-4502
1965
Pseudomonas sp., Pseudomonas sp. G6
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Metzger, R.P.; Wick, A.N.
Partial purification of rat liver D-arabinose dehydrogenase
Biochem. Biophys. Res. Commun.
26
742-747
1967
Rattus norvegicus
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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)
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