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Literature summary for 1.1.5.2 extracted from

  • Elias, M.D.; Tanaka, M.; Izu, H.; Matsushita, K.; Adachi, O.; Yamada, M.
    Functions of amino acid residues in the active site of Escherichia coli pyrroloquinoline quinone-containing quinoprotein glucose dehydrogenase (2000), J. Biol. Chem., 275, 7321-7326.
    View publication on PubMed
Search for more literature for 1.1.5.2

Protein Variants

Protein Variants Comment Organism
D466E very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme Escherichia coli
D466N very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone Escherichia coli
H262A reduced affinity both for glucose, 11fold, and pyrroloquinoline quinone, 8fold, without significant effect on glucose oxidase activity Escherichia coli
K493A very low glucose oxidase activity, without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type Escherichia coli
K493R pronounced reduction of affinity for pyrroloquinoline quinone, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type Escherichia coli
W404A pronounced reduction of affinity for pyrroloquinoline quinone, very low glucose oxidase activity and phenazine methosulfate reductase activity compared with wild-type enzyme Escherichia coli
W404F pronounced reduction of affinity for pyrroloquinoline quinone, very weak activity of phenazine methosulfate reductase but still retains glucose oxidase activity equivalent to that of the wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00005
-
 pyrroloquinoline quinone ,pH 7.0, 25°C, mutant K493A Escherichia coli
0.00011
-
 pyrroliquinoline quinone pH 7.0, 25°C, wild-type enzyme Escherichia coli
0.00014
-
 pyrroloquinoline quinone pH 7.0, 21°C, mutant D466E and D466N Escherichia coli
0.00022
-
 pyrroloquinoline quinone pH 7.0, 25°C, mutant W607A Escherichia coli
0.00088
-
 pyrroloquinoline quinone pH 7.0, 25°C, mutant H262A Escherichia coli
0.006
-
 pyrroloquinoline quinone pH 7.0, 25°C, mutant W404A Escherichia coli
0.016
-
 pyrroloquinoline quinone pH 7.0, 25°C, mutant K493R Escherichia coli
0.02
-
 pyrroloquinoline quinone pH 7.0, 25°C, mutant W404F Escherichia coli
0.8
-
 D-glucose pH 7.0, 25°C, mutant enzyme N607A Escherichia coli
0.9
-
 D-glucose pH 7.0, 25°C, wild-type enzyme Escherichia coli
1.2
-
 D-glucose pH 7.0, 25°C, mutant W404A Escherichia coli
1.4
-
 D-glucose pH 7.0, 25°C, mutant K493A Escherichia coli
1.5
-
 D-glucose pH 7.0, 25°C, mutant K493R Escherichia coli
2
-
 D-glucose pH 7.0, 21°C, mutant W404F Escherichia coli
3
-
 D-glucose pH 7.0, 25°C, mutant D466E Escherichia coli
10
-
 D-glucose pH 7.0, 25°C, mutant H262A Escherichia coli
12
-
 D-glucose pH 7.0, 25°C, mutant D466N Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone prosthetic group Escherichia coli