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Literature summary extracted from

  • Yamada, M.; Inbe, H.; Tanaka, M.; Sumi, K.; Matsushita, K.; Adachi, O.
    Mutant isolation of the Escherichia coli quinoprotein glucose dehydrogenase and analysis of crucial residues Asp-730 and His-775 for its function (1998), J. Biol. Chem., 273, 22021-22027.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.2
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 D730A low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate Escherichia coli
1.1.5.2 D730N low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate Escherichia coli
1.1.5.2 D730R reduced affnity for pyrroloquinoline quinone Escherichia coli
1.1.5.2 E742G/P757L slightly higher Km value for Mg2+ Escherichia coli
1.1.5.2 G689D significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+ Escherichia coli
1.1.5.2 H775A pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone Escherichia coli
1.1.5.2 H775R pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone, 230fold higher Km than wild-type enzyme Escherichia coli
1.1.5.2 S357L significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+ Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.2 0.00009
-
 pyrroloquinoline quinone 25°C, wild-type enzyme Escherichia coli
1.1.5.2 0.00012
-
 pyrroloquinoline quinone 25°C, mutant enzyme D730N Escherichia coli
1.1.5.2 0.0005
-
 pyrroloquinoline quinone 25°C, mutant enzyme S357L Escherichia coli
1.1.5.2 0.00064
-
 pyrroloquinoline quinone 25°C, mutant enzyme G689D Escherichia coli
1.1.5.2 0.021
-
 pyrroloquinoline quinone 25°C, mutant enzyme H775R Escherichia coli
1.1.5.2 0.8
-
 D-glucose 25°C, mutant enzyme D730 N Escherichia coli
1.1.5.2 0.91
-
 D-glucose 25°C, wild-type enzyme Escherichia coli
1.1.5.2 1
-
 D-glucose 25°C, mutant enzyme S357L Escherichia coli
1.1.5.2 1.3
-
 D-glucose 25°C, mutant enzyme H775R Escherichia coli
1.1.5.2 1.4
-
 D-glucose 25°C, mutant enzyme G689D Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.2 Mg2+ Km: 0.022 mM for the wild-type enzyme Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.2 mutant enzymes Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 D-glucose + pyrroloquinoline quinone
-
 Escherichia coli D-glucono-1,5-lactone + pyrroloquinoline quinol
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone prosthetic group Escherichia coli