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Literature summary for 1.1.1.11 extracted from
- 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 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.05 | - |
NAD+ | pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+ | Gluconobacter sp. JX-05 |  |
| 0.21 | - |
NADH | pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH | Gluconobacter sp. JX-05 | |
| 3.8 | - |
D-arabitol | pH 8.5, 30°C, recombinant His-tagged enzyme, with NAD+ | Gluconobacter sp. JX-05 | |
| 28.1 | - |
D-xylulose | pH 5.5, 30°C, recombinant His-tagged enzyme, with NADH | Gluconobacter sp. JX-05 | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-arabinitol + NAD+ | Gluconobacter sp. JX-05 | - |
D-xylulose + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gluconobacter sp. JX-05 | A0A2K9VPX3 | isolated from a sample of vinegar residue | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.7 | - |
pH 8.5, 30°C, substrates ethanol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 4.7 | - |
pH 8.5, 30°C, substrates meso-erythritol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 5.5 | - |
pH 8.5, 30°C, substrates glycerol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 7.7 | - |
pH 8.5, 30°C, substrates xylitol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 9 | - |
pH 8.5, 30°C, substrates D-sorbitol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 12.6 | - |
pH 5.5, 30°C, substrates D-fructose and NADH, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 22.9 | - |
pH 5.5, 30°C, substrates D-xylulose and NADH, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 26.8 | - |
pH 8.5, 30°C, substrates D-mannitol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 87.7 | - |
pH 8.5, 30°C, substrates D-arabitol and NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-arabinitol + NAD+ | - |
Gluconobacter sp. JX-05 | D-xylulose + NADH + H+ | - |
r | |
| D-arabitol + NAD+ | best substrates in both reaction directions | Gluconobacter sp. JX-05 | D-xylulose + NADH + H+ | - |
r | |
| D-arabitol + NADP+ | - |
Gluconobacter sp. JX-05 | D-xylulose + NADPH + H+ | - |
r | |
| 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 | |
| D-sorbitol + NAD+ | 10.3% activity with D-sorbitol compared to D-arabitol | Gluconobacter sp. JX-05 | sorbose + NADH + H+ | - |
r | |
| ethanol + NAD+ | 1.9% activity with D-sorbitol compared to D-arabitol | Gluconobacter sp. JX-05 | acetaldehyde + NADH + H+ | - |
? | |
| glycerol + NAD+ | 6.2% activity with D-sorbitol compared to D-arabitol | Gluconobacter sp. JX-05 | dihydroxyacetone + NADH + H+ | - |
? | |
| meso-erythritol + NAD+ | 5.3% activity with D-sorbitol compared to D-arabitol | Gluconobacter sp. JX-05 | L-erythrose + NADH + H+ | - |
? | |
| xylitol + NAD+ | 8.8% activity with D-sorbitol compared to D-arabitol | Gluconobacter sp. JX-05 | D-xylulose + NADH + H+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ArDH | - |
Gluconobacter sp. JX-05 |
| D-arabitol dehydrogenase | - |
Gluconobacter sp. JX-05 |
| NAD-dependent D-arabitol dehydrogenase | - |
Gluconobacter sp. JX-05 |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
both reaction directions, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
reduction of D-xylulose with NADH, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 8.5 | - |
oxidation of D-arabitol with NAD+, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 7 | reduction of D-xylulose with NADH, over 80% of maximal activity within this range, recombinant His-tagged enzyme | Gluconobacter sp. JX-05 |
| 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
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | the enzyme harbors the NAD(P)-binding motif TGXXXGXG, preferred substrate | Gluconobacter sp. JX-05 | |
| NADH | preferred substrate | Gluconobacter sp. JX-05 | |
| NADP+ | - |
Gluconobacter sp. JX-05 | |
| NADPH | - |
Gluconobacter sp. JX-05 | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
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