Protein Variants | Comment | Organism |
---|---|---|
D354N | site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | Escherichia coli |
D354N/N355D | site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | Escherichia coli |
N355D | site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | competitive to Mg2+, wild-type enzyme | Escherichia coli | |
Ca2+ | competitive to Mg2+, wild-type enzyme | Escherichia coli | |
Mg2+ | competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D | Escherichia coli | |
Sr2+ | competitive to Mg2+, wild-type enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview | Escherichia coli | |
2.8 | - |
D-glucose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
3.5 | - |
2-deoxy-D-glucose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
17 | - |
D-xylose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
17.5 | - |
D-galactose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
31 | - |
L-arabinose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
79 | - |
3-O-methyl-D-glucose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
116 | - |
D-mannose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli | |
166 | - |
D-ribose | recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
periplasm | - |
Escherichia coli | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | mutants D354N, N355D, and D354N/N355D | Escherichia coli | |
Ca2+ | mutants D354N, N355D, and D354N/N355D | Escherichia coli | |
Mg2+ | required, bound at the active site, cannot be substituted by Ca2+, Sr2+, or Ba2+ | Escherichia coli | |
Sr2+ | mutants D354N, N355D, and D354N/N355D | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose + ubiquinone | Escherichia coli | transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain | D-glucono-1,5-lactone + ubiquinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P15877 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol | active site structure | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-deoxy-D-glucose + ubiquinone | - |
Escherichia coli | 2-deoxy-D-glucono-1,5-lactone + ubiquinol | - |
? | |
3-O-methyl-D-glucose + ubiquinone | - |
Escherichia coli | 3-O-methyl-D-glucono-1,5-lactone + ubiquinol | - |
? | |
D-galactose + ubiquinone | - |
Escherichia coli | D-galactono-1,5-lactone + ubiquinol | - |
? | |
D-glucose + ubiquinone | - |
Escherichia coli | D-glucono-1,5-lactone + ubiquinol | - |
? | |
D-glucose + ubiquinone | transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain | Escherichia coli | D-glucono-1,5-lactone + ubiquinol | - |
? | |
D-mannose + ubiquinone | - |
Escherichia coli | ? + ubiquinol | - |
? | |
D-ribose + ubiquinone | - |
Escherichia coli | ? + ubiquinol | - |
? | |
D-xylose + ubiquinone | - |
Escherichia coli | D-xylono-1,5-lactone + ubiquinol | - |
? | |
L-arabinose + ubiquinone | - |
Escherichia coli | L-arabino-1,5-lactone + ubiquinol | - |
? | |
additional information | substrate specificity of recombinant wild-type and mutant enzymes | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GDH | - |
Escherichia coli |
membrane glucose dehydrogenase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40.5 | - |
10 min, 50% inactivation of recombinant mutant D354N apoenzyme | Escherichia coli |
40.8 | - |
10 min, 50% inactivation of recombinant wild-type apoenzyme | Escherichia coli |
41 | - |
10 min, 50% inactivation of recombinant mutant D354N/N355D apoenzyme | Escherichia coli |
43.2 | - |
10 min, 50% inactivation of recombinant mutant N355D apoenzyme | Escherichia coli |
48.6 | - |
10 min, 50% inactivation of recombinant mutant D354N/N355D holoenzyme | Escherichia coli |
49 | - |
10 min, 50% inactivation of recombinant mutant D354N holoenzyme | Escherichia coli |
51 | - |
10 min, 50% inactivation of recombinant wild-type holoenzyme | Escherichia coli |
55 | - |
10 min, 50% inactivation of recombinant mutant N355D holoenzyme | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibitory effects of the different metal ions on recombinant wild-type and mutant enzymes | Escherichia coli |