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Literature summary for 1.1.5.2 extracted from

  • Geiger, O.; Goerisch, H.
    Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus (1989), Biochem. J., 261, 415-421.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.5.2

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ pyrroloquinoline quinone is bound at the active site via a Ca2+ bridge, enzyme contains 1.95 mol of Ca2+ per mol of subunit Acinetobacter calcoaceticus
Ca2+ Ca2+ is required for reactivation after thermal inactivation Acinetobacter calcoaceticus
Cd2+ can replace Ca2+ in reactivation after thermal inactivation Acinetobacter calcoaceticus
Mn2+ can replace Ca2+ in reactivation after thermal inactivation Acinetobacter calcoaceticus

Organism

Organism UniProt Comment Textmining
Acinetobacter calcoaceticus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + pyrroloquinoline quinone
-
 Acinetobacter calcoaceticus D-glucono-1,5-lactone + pyrroloquinoline quinol
-
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
 pH 6, 10 min, in absence of Ca2+, stable below, reversible inactivation above Acinetobacter calcoaceticus
50
-
 pH 6, 10 min, in presence of Ca2+, inactivation above Acinetobacter calcoaceticus