Application | Comment | Organism |
---|---|---|
analysis | because of its high turnover number, PQQ-GDH is proposed as an enzyme label for the development of sensitive electrochemical enzyme-amplified bioaffinity assays. It has, for example, been applied to the amperometric detection of DNA hybrids or sandwich DNA aptamers at the surface of a carbon electrode | Acinetobacter calcoaceticus |
Protein Variants | Comment | Organism |
---|---|---|
N428C | site-directed mutagenesis, at relatively high concentrations of mediator and substrate, catalysis by the mutant type may be more efficient than with the wild-type | Acinetobacter calcoaceticus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-glucose | substrate inhibition | Acinetobacter calcoaceticus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview | Acinetobacter calcoaceticus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+ | Acinetobacter calcoaceticus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose + ubiquinone | Acinetobacter calcoaceticus | - |
D-glucono-1,5-lactone + ubiquinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter calcoaceticus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol | ping pong reaction mechanism | Acinetobacter calcoaceticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose + ubiquinone | - |
Acinetobacter calcoaceticus | D-glucono-1,5-lactone + ubiquinol | - |
? | |
additional information | PQQ-GDH has a broad specificity toward the oxidation of aldose sugars (hexoses, pentoses, mono- and disaccharides) into the corresponding lactones and the reduction of artificial electron acceptors | Acinetobacter calcoaceticus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+ | Acinetobacter calcoaceticus |
Synonyms | Comment | Organism |
---|---|---|
PQQ-GDH | - |
Acinetobacter calcoaceticus |
quinoprotein glucose dehydrogenase | - |
Acinetobacter calcoaceticus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1550 | - |
D-glucose | pH 7.0, temperature not specified in the publication, wild-type enzyme | Acinetobacter calcoaceticus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Acinetobacter calcoaceticus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+ | Acinetobacter calcoaceticus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2100 | - |
D-glucose | pH 7.0, temperature not specified in the publication, wild-type enzyme | Acinetobacter calcoaceticus |