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IUBMB Comments The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
The enzyme appears in viruses and cellular organisms
Synonyms
apsD , D-apiose reductase,
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D-apiose reductase
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D-apiofuranose + NAD+ = D-apionolactone + NADH + H+
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D-apiofuranose:NAD+ 1-oxidoreductase
The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
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D-apiitol + NAD+
D-apiose + NADH + H+
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r
D-apiofuranose + NAD+
D-apionolactone + NADH + H+
D-apiose + NADH + H+
D-apiitol + NAD+
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r
D-erythrose + NADH + H+
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1.5% activity compared to D-apiose
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ribitol + NAD+
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5.5% activity compared to D-apiitol
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additional information
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D-apiofuranose + NAD+
D-apionolactone + NADH + H+
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r
D-apiofuranose + NAD+
D-apionolactone + NADH + H+
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r
D-mannitol + NAD+
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1.0% activity compared to D-apiitol
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D-mannitol + NAD+
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1.0% activity compared to D-apiitol
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D-ribulose + NADH + H+
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8.5% activity compared to D-apiose
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D-ribulose + NADH + H+
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8.5% activity compared to D-apiose
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erythritol + NAD+
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1.0% activity compared to D-apiitol
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erythritol + NAD+
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1.0% activity compared to D-apiitol
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additional information
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the enzyme is almost completely specific for the reduced and oxidized forms of nicotinamide adenine dinucleotide. The activity obtained with NADPH and NADP+ is 1.5 and 0.9%, respectively, of that obtained with NADH and NAD+
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additional information
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no activity is obtained with D-glucose, D-mannose, D-galactose, D-fructose, L-rhamnose, L-fucose, D-ribose, D-xylose, L-arabinose, D-arabinose, D-xylulose, D-glyceraldehyde, galactitol, sorbitol, xylitol, L-arabitol, D-arabitol, and glycerol
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additional information
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the enzyme is almost completely specific for the reduced and oxidized forms of nicotinamide adenine dinucleotide. The activity obtained with NADPH and NADP+ is 1.5 and 0.9%, respectively, of that obtained with NADH and NAD+
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additional information
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no activity is obtained with D-glucose, D-mannose, D-galactose, D-fructose, L-rhamnose, L-fucose, D-ribose, D-xylose, L-arabinose, D-arabinose, D-xylulose, D-glyceraldehyde, galactitol, sorbitol, xylitol, L-arabitol, D-arabitol, and glycerol
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D-apiofuranose + NAD+
D-apionolactone + NADH + H+
D-apiose + NADH + H+
D-apiitol + NAD+
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r
additional information
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D-apiofuranose + NAD+
D-apionolactone + NADH + H+
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r
D-apiofuranose + NAD+
D-apionolactone + NADH + H+
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r
additional information
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the enzyme is almost completely specific for the reduced and oxidized forms of nicotinamide adenine dinucleotide. The activity obtained with NADPH and NADP+ is 1.5 and 0.9%, respectively, of that obtained with NADH and NAD+
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additional information
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the enzyme is almost completely specific for the reduced and oxidized forms of nicotinamide adenine dinucleotide. The activity obtained with NADPH and NADP+ is 1.5 and 0.9%, respectively, of that obtained with NADH and NAD+
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NAD+
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NADH
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additional information
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enzymatic reduction of D-apiose is not appreciably affected by the presence of 0.02 M EDTA
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0.01
D-apiitol
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at pH 9.5 and 25°C
0.02
D-apiose
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at pH 7.5 and 25°C
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10.5
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optimal activity for the oxidation of D-apiitol is obtained at pH 10.5 in glycine buffer
6.5
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optimal activity for the reduction of D-apiose is obtained at pH 7.5 in sodium phosphate buffer
7.5
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optimal activity for the reduction of D-apiose is obtained at pH 7.5 in glycylglycine buffer
9.5
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optimal activity for the oxidation of D-apiitol is obtained at pH 10.5 in glycylglycine buffer
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UniProt
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UniProt
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brenda
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APSD_AGRRK
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
345
0
37447
Swiss-Prot
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APSD_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
375
0
40406
Swiss-Prot
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the presence of 0.06 M mercaptoethanol increases the stability of the enzyme when stored at 0-4 °C
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0-4°C, storage medium, 24 h, 10-20% loss of activity
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0-4°C, storage medium, 48 h, 50% loss of activity
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Ni-NTA resin column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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Neal, D.L.; Kindel, P.K.
D-apiose reductase from Aerobacter aerogenes
J. Bacteriol.
101
910-915
1970
Klebsiella aerogenes, Klebsiella aerogenes PRL-R3
brenda
Carter, M.; Zhang, X.; Huang, H.; Bouvier, J.; Francisco, B.; Vetting, M.; Al-Obaidi, N.; Bonanno, J.; Ghosh, A.; Zallot, R.; Andersen, H.; Almo, S.; Gerlt, J.
Functional assignment of multiple catabolic pathways for D-apiose article
Nat. Chem. Biol.
14
696-705
2018
Agrobacterium tumefaciens (B9JK80), Agrobacterium tumefaciens K84 (B9JK80)
brenda
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