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Literature summary for 1.1.5.2 extracted from
- Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus (1996), Arch. Biochem. Biophys., 336, 42-48.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the apoenzyme in Escherichia coli | Acinetobacter calcoaceticus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Acinetobacter calcoaceticus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required for dimerization of the subunits as well as for functionalization of the bound pyrroloquinoline quinone. Binding of Ca2+ is much stronger in the holoenzyme than in the apoenzyme | Acinetobacter calcoaceticus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter calcoaceticus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Acinetobacter calcoaceticus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 7400 | - |
recombinant enzyme | Acinetobacter calcoaceticus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyrroloquinoline quinone | prosthetic group | Acinetobacter calcoaceticus | |
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