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Literature summary extracted from

  • James, P.L.; Anthony, C.
    The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli (2003), Biochim. Biophys. Acta, 1647, 200-205.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 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
1.1.5.2 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
1.1.5.2 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

EC Number Inhibitors Comment Organism Structure
1.1.5.2 Ba2+ competitive to Mg2+, wild-type enzyme Escherichia coli
1.1.5.2 Ca2+ competitive to Mg2+, wild-type enzyme Escherichia coli
1.1.5.2 Mg2+ competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D Escherichia coli
1.1.5.2 Sr2+ competitive to Mg2+, wild-type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.2 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
1.1.5.2 2.8
-
D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 3.5
-
2-deoxy-D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 17
-
D-xylose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 17.5
-
D-galactose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 31
-
L-arabinose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 79
-
3-O-methyl-D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 116
-
D-mannose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
1.1.5.2 166
-
D-ribose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 membrane
-
Escherichia coli 16020
-
1.1.5.2 periplasm
-
Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.2 Ba2+ mutants D354N, N355D, and D354N/N355D Escherichia coli
1.1.5.2 Ca2+ mutants D354N, N355D, and D354N/N355D Escherichia coli
1.1.5.2 Mg2+ required, bound at the active site, cannot be substituted by Ca2+, Sr2+, or Ba2+ Escherichia coli
1.1.5.2 Sr2+ mutants D354N, N355D, and D354N/N355D Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.2 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

EC Number Organism UniProt Comment Textmining
1.1.5.2 Escherichia coli P15877
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.5.2 D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol active site structure Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 2-deoxy-D-glucose + ubiquinone
-
Escherichia coli 2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
?
1.1.5.2 3-O-methyl-D-glucose + ubiquinone
-
Escherichia coli 3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
?
1.1.5.2 D-galactose + ubiquinone
-
Escherichia coli D-galactono-1,5-lactone + ubiquinol
-
?
1.1.5.2 D-glucose + ubiquinone
-
Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
?
1.1.5.2 D-glucose + ubiquinone transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
?
1.1.5.2 D-mannose + ubiquinone
-
Escherichia coli ? + ubiquinol
-
?
1.1.5.2 D-ribose + ubiquinone
-
Escherichia coli ? + ubiquinol
-
?
1.1.5.2 D-xylose + ubiquinone
-
Escherichia coli D-xylono-1,5-lactone + ubiquinol
-
?
1.1.5.2 L-arabinose + ubiquinone
-
Escherichia coli L-arabino-1,5-lactone + ubiquinol
-
?
1.1.5.2 additional information substrate specificity of recombinant wild-type and mutant enzymes Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.2 GDH
-
Escherichia coli
1.1.5.2 membrane glucose dehydrogenase
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.2 25
-
assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.2 40.5
-
10 min, 50% inactivation of recombinant mutant D354N apoenzyme Escherichia coli
1.1.5.2 40.8
-
10 min, 50% inactivation of recombinant wild-type apoenzyme Escherichia coli
1.1.5.2 41
-
10 min, 50% inactivation of recombinant mutant D354N/N355D apoenzyme Escherichia coli
1.1.5.2 43.2
-
10 min, 50% inactivation of recombinant mutant N355D apoenzyme Escherichia coli
1.1.5.2 48.6
-
10 min, 50% inactivation of recombinant mutant D354N/N355D holoenzyme Escherichia coli
1.1.5.2 49
-
10 min, 50% inactivation of recombinant mutant D354N holoenzyme Escherichia coli
1.1.5.2 51
-
10 min, 50% inactivation of recombinant wild-type holoenzyme Escherichia coli
1.1.5.2 55
-
10 min, 50% inactivation of recombinant mutant N355D holoenzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.2 6.5
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.5.2 additional information
-
additional information inhibitory effects of the different metal ions on recombinant wild-type and mutant enzymes Escherichia coli