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Literature summary extracted from

  • Qi, X.; Zhang, H.; Magocha, T.A.; An, Y.; Yun, J.; Yang, M.; Xue, Y.; Liang, S.; Sun, W.; Cao, Z.
    Improved xylitol production by expressing a novel D-arabitol dehydrogenase from isolated Gluconobacter sp. JX-05 and co-biotransformation of whole cells (2017), Biores. Technol., 235, 50-58 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.11 gene ardh, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Gluconobacter sp. JX-05

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.11 additional information in the co-biotransformation by the whole cells of recombinant Escherichia coli BL21(DE3)-ardh and BL21(DE3)-xdh strains, 26.1 g/l xylitol is produced from 30 g/l D-arabitol in 22 h with a yield 0.87 g/g. The xylitol production is increased by more than two times as compared with that of Gluconobacter sp. alone, and is improved 10.1% than that of Gluconobacter sp. mixed with Escherichia coli strain BL21(DE3)-xdh Gluconobacter sp. JX-05

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.11 0.05
-
 NAD+ pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+ Gluconobacter sp. JX-05
1.1.1.11 0.21
-
 NADH pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH Gluconobacter sp. JX-05
1.1.1.11 3.8
-
 D-arabitol pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+ Gluconobacter sp. JX-05
1.1.1.11 28.1
-
 D-xylulose pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH Gluconobacter sp. JX-05

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.11 D-arabinitol + NAD+ Gluconobacter sp. JX-05
-
 D-xylulose + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.11 Gluconobacter sp. JX-05 A0A2K9VPX3 isolated from a sample of vinegar residue
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.11 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Gluconobacter sp. JX-05

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.11 1.7
-
 pH 8.5, 30°C, substrates ethanol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 4.7
-
 pH 8.5, 30°C, substrates meso-erythritol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 5.5
-
 pH 8.5, 30°C, substrates glycerol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 7.7
-
 pH 8.5, 30°C, substrates xylitol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 9
-
 pH 8.5, 30°C, substrates D-sorbitol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 12.6
-
 pH 5.5, 30°C, substrates D-fructose and NADH, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 22.9
-
 pH 5.5, 30°C, substrates D-xylulose and NADH, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 26.8
-
 pH 8.5, 30°C, substrates D-mannitol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 87.7
-
 pH 8.5, 30°C, substrates D-arabitol and NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.11 D-arabinitol + NAD+
-
 Gluconobacter sp. JX-05 D-xylulose + NADH + H+
-
 r
1.1.1.11 D-arabitol + NAD+ best substrates in both reaction directions Gluconobacter sp. JX-05 D-xylulose + NADH + H+
-
 r
1.1.1.11 D-arabitol + NADP+
-
 Gluconobacter sp. JX-05 D-xylulose + NADPH + H+
-
 r
1.1.1.11 D-mannitol + NAD+ 30.5% and 54.8% activity with D-mannitol and D-fructose compared to D-arabitol and D-xylulose, respectively Gluconobacter sp. JX-05 D-fructose + NADH + H+
-
 r
1.1.1.11 D-sorbitol + NAD+ 10.3% activity with D-sorbitol compared to D-arabitol Gluconobacter sp. JX-05 sorbose + NADH + H+
-
 r
1.1.1.11 ethanol + NAD+ 1.9% activity with D-sorbitol compared to D-arabitol Gluconobacter sp. JX-05 acetaldehyde + NADH + H+
-
 ?
1.1.1.11 glycerol + NAD+ 6.2% activity with D-sorbitol compared to D-arabitol Gluconobacter sp. JX-05 dihydroxyacetone + NADH + H+
-
 ?
1.1.1.11 meso-erythritol + NAD+ 5.3% activity with D-sorbitol compared to D-arabitol Gluconobacter sp. JX-05 L-erythrose + NADH + H+
-
 ?
1.1.1.11 xylitol + NAD+ 8.8% activity with D-sorbitol compared to D-arabitol Gluconobacter sp. JX-05 D-xylulose + NADH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.11 ArDH
-
 Gluconobacter sp. JX-05
1.1.1.11 D-arabitol dehydrogenase
-
 Gluconobacter sp. JX-05
1.1.1.11 NAD-dependent D-arabitol dehydrogenase
-
 Gluconobacter sp. JX-05

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.11 30
-
 both reaction directions, recombinant His-tagged enzyme Gluconobacter sp. JX-05

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.11 25 55 oxidation and reduction activities of ArDH, over 80% of maximal activity at 24-40°C, and below 60% of maximal activity when the temperature exceeds 55°C, recombinant His-tagged enzyme Gluconobacter sp. JX-05

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.11 5.5
-
 reduction of D-xylulose with NADH, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 8.5
-
 oxidation of D-arabitol with NAD+, recombinant His-tagged enzyme Gluconobacter sp. JX-05

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.11 3 7 reduction of D-xylulose with NADH, over 80% of maximal activity within this range, recombinant His-tagged enzyme Gluconobacter sp. JX-05
1.1.1.11 6 11 oxidation of D-arabitol with NAD+, over 60% of maximal activity within this range, recombinant His-tagged enzyme Gluconobacter sp. JX-05

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.11 NAD+ the enzyme harbors the NAD(P)-binding motif TGXXXGXG, preferred substrate Gluconobacter sp. JX-05
1.1.1.11 NADH preferred substrate Gluconobacter sp. JX-05
1.1.1.11 NADP+
-
 Gluconobacter sp. JX-05
1.1.1.11 NADPH
-
 Gluconobacter sp. JX-05

General Information

EC Number General Information Comment Organism
1.1.1.11 evolution enzyme ArDH containing a NAD(P)-binding motif TGXXX[AG]XG and a classical active site motif belongs to the short-chain dehydrogenase family Gluconobacter sp. JX-05
1.1.1.11 additional information ArDH has a conserved sequence region of TGXXXGXG, in this NAD(P)-binding motif, glycine-rich region plays a critical role in the stability of this kind of domain. Conserved domain of YXXXK, a classical active site motif, accompanying with two conserved amino acids N119 and S147 in the upstream, is also found in ArDH, sequence comparisons. Structure-function analysis of ArDH, and structure homology modeling using the structure of putative polyol dehydrogenase (PDB ID 3AWD) from Gluconobacter oxydans strain DSM2343 as template, overview Gluconobacter sp. JX-05