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Literature summary extracted from

  • Yamada, M.; Elias, M.D.; Matsushita, K.; Migita, C.T.; Adachi, O.
    Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins (2003), Biochim. Biophys. Acta, 1647, 185-192.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 cytoplasm soluble enzyme sGDH Acinetobacter calcoaceticus 5737
-
1.1.5.2 membrane bound, enzyme mGDH Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.2 Ca2+ required, interacts with PQQ cofactor Escherichia coli
1.1.5.2 Ca2+ required, interacts with PQQ cofactor Acinetobacter calcoaceticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.2 D-glucose + ? Acinetobacter calcoaceticus physiological electron acceptor in not known D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 D-glucose + ubiquinone Escherichia coli a pivotal PQQ-containing quinoprotein coupled to the respiratory chain in the periplasmic oxidation of alcohols and sugars D-glucono-1,5-lactone + ubiquinol
-
 ?
1.1.5.2 additional information Escherichia coli evolutionary analysis of PQQ-containing proteins, overview ?
-
 ?
1.1.5.2 additional information Acinetobacter calcoaceticus evolutionary analysis of PQQ-containing proteins, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Acinetobacter calcoaceticus P13650
-
-
1.1.5.2 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.5.2 D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol active site structure Acinetobacter calcoaceticus
a
1.1.5.2 D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol active site structure, putative catalytic mechanism and cycle involving Asp466 and Lys493 Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 D-glucose + ? physiological electron acceptor in not known Acinetobacter calcoaceticus D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 D-glucose + ubiquinone
-
 Acinetobacter calcoaceticus D-glucono-1,5-lactone + ubiquinol
-
 ?
1.1.5.2 D-glucose + ubiquinone a pivotal PQQ-containing quinoprotein coupled to the respiratory chain in the periplasmic oxidation of alcohols and sugars Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
 ?
1.1.5.2 D-glucose + ubiquinone with ubiquinone-8 as minor compound, PQQ acts in electron transfer between enzyme and ubiquinone Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
 ?
1.1.5.2 additional information evolutionary analysis of PQQ-containing proteins, overview Escherichia coli ?
-
 ?
1.1.5.2 additional information evolutionary analysis of PQQ-containing proteins, overview Acinetobacter calcoaceticus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.5.2 dimer (alpha)2, functional subunit composition, domain and overall structure analysis Acinetobacter calcoaceticus
1.1.5.2 monomer functional subunit composition, domain and overall structure analysis Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.1.5.2 glucose dehydrogenase
-
 Escherichia coli
1.1.5.2 glucose dehydrogenase
-
 Acinetobacter calcoaceticus
1.1.5.2 mGDH
-
 Escherichia coli
1.1.5.2 sGDH
-
 Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone i.e. PQQ, dependent on Acinetobacter calcoaceticus
1.1.5.2 pyrroloquinoline quinone i.e. PQQ, dependent on exogenous PQQ, since Escherichia coli does not synthesize PQQ itself Escherichia coli