Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.5.2 extracted from

  • Iswantini, D.; Kano, K.; Ikeda, T.
    Kinetics and thermodynamics of activation of quinoprotein glucose dehydrogenase apoenzyme in vivo and catalytic activity of the activated enzyme in Escherichia coli cells (2000), Biochem. J., 350, 917-923.
No PubMed abstract available
Search for more literature for 1.1.5.2

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound to Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ catalytic activity of the membrane-bound enzyme with Ca2+ is very similar to that with Mg2+ Escherichia coli
Mg2+ the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+. Mg2+ allows the cofactor to take a more appropriate position in the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
 Escherichia coli D-glucono-1,5-lactone + ?
-
 ?
D-glucose + 2,6-dichlorophenol-indophenol
-
 Escherichia coli D-glucono-1,5-lactone + ?
-
 ?
D-glucose + ferricyanide
-
 Escherichia coli D-glucono-1,5-lactone + ferrocyanide
-
 ?
D-glucose + phenazine methosulfate
-
 Escherichia coli D-glucono-1,5-lactone + ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone prosthetic group Escherichia coli
pyrroloquinoline quinone the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+ Escherichia coli