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Literature summary extracted from
- Secretion of water soluble pyrroloquinoline quinone glucose dehydrogenase by recombinant Pichia pastoris (2002), Enzyme Microb. Technol., 30, 312-318.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.1.5.2 | biotechnology | optimization of an expression system using Pichia pastoris for use in industrial level production | Acinetobacter calcoaceticus |
| 1.1.99.35 | synthesis | expression of enzyme in Pichia pastoris using the Saccharomyces cerevisiae alpha-factor signal sequence for secretion. The productivity of secreted PQQGDH-B achieves 218 kU/liter, i.e. 43 mg/liter. The secreted PQQGDH-B in Pichia pastoris is glycosylated but shows similar enzymatic properties as compared with those of recombinant PQQGDH-B produced in Escherichia coli | Acinetobacter calcoaceticus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.5.2 | expression of isozyme PQQGDH-B, in Pichia pastoris using the alpha-factor signal sequence of Saccharomyces cerevisiae, recombinant enzyme is secreted to the medium, optimization of enzyme production | Acinetobacter calcoaceticus |
| 1.1.99.35 | expression in Pichia pastoris | Acinetobacter calcoaceticus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.99.35 | additional information | expression in Pichia pastoris using the Saccharomyces cerevisiae alpha-factor signal sequence for secretion. The productivity of secreted PQQGDH-B achieves 218 kU/liter, i.e. 43 mg/liter. The secreted PQQGDH-B in Pichia pastoris is glycosylated but shows similar enzymatic properties as compared with those of recombinant PQQGDH-B produced in Escherichia coli | Acinetobacter calcoaceticus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.5.2 | additional information | poor inhibition of isozyme PQQGDH-B by 5 mM EDTA | Acinetobacter calcoaceticus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.99.35 | 17.5 | - |
D-glucose | recombinant enzyme, expression in Pichia pastoris | Acinetobacter calcoaceticus |  |
| 1.1.99.35 | 17.5 | - |
lactose | recombinant enzyme, expression in Pichia pastoris | Acinetobacter calcoaceticus | |
| 1.1.99.35 | 18.9 | - |
lactose | recombinant enzyme, expression in Escherichia coli | Acinetobacter calcoaceticus | |
| 1.1.99.35 | 25 | - |
D-glucose | recombinant enzyme, expression in Escherichia coli | Acinetobacter calcoaceticus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.1.5.2 | membrane | isozyme PQQGDH-A | Acinetobacter calcoaceticus | 16020 | - |
| 1.1.5.2 | periplasm | - |
Acinetobacter calcoaceticus | - |
- |
| 1.1.5.2 | soluble | isozyme PQQGDH-B | Acinetobacter calcoaceticus | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.5.2 | 50000 | - |
2 * 50000, deglycosylated recombinant isozyme PQQGDH-B, SDS-PAGE | Acinetobacter calcoaceticus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.5.2 | Acinetobacter calcoaceticus | - |
2 isozymes PQQGDH-A and PQQGDH-B | - |
| 1.1.99.35 | Acinetobacter calcoaceticus | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.1.5.2 | glycoprotein | secreted recombinant isozyme PQQGDH-B expressed in Pichia pastoris | Acinetobacter calcoaceticus |
| 1.1.99.35 | glycoprotein | the secreted PQQGDH-B in Pichia pastoris is glycosylated but shows similar enzymatic properties as compared with those of recombinant PQQGDH-B produced in Escherichia coli | Acinetobacter calcoaceticus |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.5.2 | recombinant isozyme PQQGDH-B from Pichia pastoris culture medium, optimization of down-stream processing | Acinetobacter calcoaceticus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.1.5.2 | 5080 | - |
purified recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.5.2 | 2-deoxy-D-glucose + ubiquinone | low activity, recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | 2-deoxy-D-glucono-1,5-lactone + ubiquinol | - |
? | |
| 1.1.5.2 | 3-O-methyl-D-glucose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | 3-O-methyl-D-glucono-1,5-lactone + ubiquinol | - |
? | |
| 1.1.5.2 | allose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | ? + ubiquinol | - |
? | |
| 1.1.5.2 | cellobiose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | ? + ubiquinol | - |
? | |
| 1.1.5.2 | D-galactose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | D-galactono-1,5-lactone + ubiquinol | - |
? | |
| 1.1.5.2 | D-glucose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | D-glucono-1,5-lactone + ubiquinol | - |
? | |
| 1.1.5.2 | D-mannose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | ? + ubiquinol | - |
? | |
| 1.1.5.2 | D-xylose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | D-xylono-1,5-lactone + ubiquinol | - |
? | |
| 1.1.5.2 | lactose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | ? + ubiquinol | - |
? | |
| 1.1.5.2 | maltose + ubiquinone | recombinant isozyme PQQGDH-B | Acinetobacter calcoaceticus | ? + ubiquinol | - |
? | |
| 1.1.5.2 | additional information | substrate specificity of the recombinant enzyme produced in Pichia pastoris | Acinetobacter calcoaceticus | ? | - |
? | |
| 1.1.99.35 | D-glucose + oxidized 2,6-dichlorophenol-indophenol | - |
Acinetobacter calcoaceticus | D-glucono-1,5-lactone + reduced 2,6-dichlorophenol-indophenol | - |
? | |
| 1.1.99.35 | lactose + oxidized 2,6-dichlorophenol-indophenol | - |
Acinetobacter calcoaceticus | ? + reduced 2,6-dichlorophenol-indophenol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.5.2 | dimer | 2 * 50000, deglycosylated recombinant isozyme PQQGDH-B, SDS-PAGE | Acinetobacter calcoaceticus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.5.2 | PQQGDH-B | - |
Acinetobacter calcoaceticus |
| 1.1.5.2 | pyrroloquinoline quinone glucose dehydrogenase | - |
Acinetobacter calcoaceticus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.5.2 | 55 | - |
isozyme PQQGDH-B, 50% residual activity after 10 min | Acinetobacter calcoaceticus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.5.2 | 7 | - |
assay at | Acinetobacter calcoaceticus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.5.2 | pyrroloquinoline quinone | prosthetic group | Acinetobacter calcoaceticus | |
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Release 2023.1 (January 2023)
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