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Literature summary for 1.1.5.2 extracted from
- Construction of engineered water-soluble PQQ glucose dehydrogenase with improved substrate specificity (2002), Biocatal. Biotransform., 20, 405-412.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | bioengineering of water-soluble isozyme PQQGDH-B production at industrial level | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant isozymes PQQGDH-B | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D448N | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| D456N | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| D457N | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N452D | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N452H | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N452I | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N452K | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N452T | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N462D | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N462H | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N462K | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
| N462Y | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.7 | - |
D-galactose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli |  |
| 3.7 | - |
D-galactose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 5.3 | - |
D-galactose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 12.3 | - |
D-glucose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 12.5 | - |
D-glucose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 16 | - |
maltose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 18 | - |
lactose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 18.9 | - |
lactose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 25 | - |
D-glucose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 26 | - |
maltose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 27.6 | - |
3-O-methyl-D-glucose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 28.7 | - |
3-O-methyl-D-glucose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 28.8 | - |
3-O-methyl-D-glucose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 32.5 | - |
allose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 33.6 | - |
lactose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 35.5 | - |
allose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 38.7 | - |
allose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 46.5 | - |
maltose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | isoyzme PQQGDH-B | Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
isozyme PQQGDH-B | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol | active site structure contains a loop 6BC region which does not directly interact with the substrates | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-O-methyl-D-glucose + ubiquinone | - |
Escherichia coli | 3-O-methyl-D-glucono-1,5-lactone + ubiquinol | - |
? | |
| allose + ubiquinone | - |
Escherichia coli | ? + ubiquinol | - |
? | |
| D-galactose + ubiquinone | low activity, recombinant wild-type and mutant isozymes PQQGDH-B | Escherichia coli | D-galactono-1,5-lactone + ubiquinol | - |
? | |
| D-glucose + ubiquinone | best substrate, recombinant wild-type and mutant isozymes PQQGDH-B | Escherichia coli | D-glucono-1,5-lactone + ubiquinol | - |
? | |
| lactose + ubiquinone | - |
Escherichia coli | ? + ubiquinol | - |
? | |
| maltose + ubiquinone | - |
Escherichia coli | ? + ubiquinol | - |
? | |
| additional information | substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | 3D-model prediction for wild-type and mutant isozyme PQQGDH-B | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PQQGDH-B | - |
Escherichia coli |
| water-soluble PQQ glucose dehydrogenase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 69 | - |
D-galactose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 72 | - |
D-galactose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 232 | - |
D-galactose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 574 | - |
lactose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 588 | - |
maltose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 949 | - |
allose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1002 | - |
maltose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1035 | - |
allose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1038 | - |
lactose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1064 | - |
3-O-methyl-D-glucose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1253 | - |
3-O-methyl-D-glucose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1399 | - |
D-glucose | N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1659 | - |
lactose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1791 | - |
D-glucose | N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 1930 | - |
maltose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 2509 | - |
allose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 3011 | - |
3-O-methyl-D-glucose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
| 3860 | - |
D-glucose | wild-type isozyme PQQGDH-B, pH 7.0, 25°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyrroloquinoline quinone | prosthetic group | Escherichia coli | |
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