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Literature summary extracted from

  • Mustafa, G.; Ishikawa, Y.; Kobayashi, K.; Migita, C.T.; Elias, M.; Nakamura, S.; Tagawa, S.; Yamada, M.
    Amino acid residues interacting both with the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase (2008), J. Biol. Chem., 283, 22215-22221.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.2 mutants are expressed in Escherichia coli YU423 cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 D354N mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity Escherichia coli
1.1.5.2 D466E mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme Escherichia coli
1.1.5.2 D466N mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme Escherichia coli
1.1.5.2 K493A mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme Escherichia coli
1.1.5.2 K493R mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 membrane
-
 Escherichia coli 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Escherichia coli
-
-
-
1.1.5.2 Escherichia coli YU423
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.2 DEAE-Toyopearl column chromatography and hydroxyapatite column chromatography Escherichia coli
1.1.5.2 using two column chromatographies of DEAE-Toyopearl and ceramic hydroxyapatite Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 D-glucose + pyrroloquinoline quinone
-
 Escherichia coli D-glucono-1,5-lactone + pyrroloquinoline quinol
-
 ?
1.1.5.2 D-glucose + pyrroloquinoline quinone
-
 Escherichia coli YU423 D-glucono-1,5-lactone + pyrroloquinoline quinol
-
 ?
1.1.5.2 phenazine methosulfate + 2,6-dichlorophenol indophenol
-
 Escherichia coli ?
-
 ?
1.1.5.2 phenazine methosulfate + 2,6-dichlorophenol indophenol
-
 Escherichia coli YU423 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.2 glucose dehydrogenase
-
 Escherichia coli
1.1.5.2 membrane-bound glucose dehydrogenase
-
 Escherichia coli
1.1.5.2 mGDH
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone
-
 Escherichia coli
1.1.5.2 pyrroloquinoline quinone coenzyme Escherichia coli

General Information

EC Number General Information Comment Organism
1.1.5.2 physiological function enzymatic analysis of purified mGDH from cells defective in synthesis of ubiquinone and/or menaquinone reveal that quinone-free mGDH has very low levels of activity of glucose dehydrogenase and UQ2 reductase compared with those of ubiquinone-bearing mGDH, both activities are increased by reconstitution with ubuquinone1. mGDH utilizes both menaquinone and ubiquinone as a bound quinine. Bound menaquinone occurs in a fashion similar to that of bound ubiquinone in the mGDH molecule and functions as an electron acceptor from pyrrolo quinoline quinone Escherichia coli