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Literature summary extracted from

  • Yamada, M.; Sumi, K.; Matsushita, K.; Adachi, O.; Yamada, Y.
    Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site (1993), J. Biol. Chem., 268, 12812-12817.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 membrane inner membrane, the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane, and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane Escherichia coli 16020
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Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.2 additional information Escherichia coli the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Escherichia coli
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-
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Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.2 211
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 D-glucose + 2,6-dichlorophenol-indophenol
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 Escherichia coli D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 additional information the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane Escherichia coli ?
-
 ?

Cofactor

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