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Literature summary for 1.1.5.2 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
Search for more literature for 1.1.5.2

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
D354N mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity Escherichia coli
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
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
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
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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli YU423
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glucose dehydrogenase
-
 Escherichia coli
membrane-bound glucose dehydrogenase
-
 Escherichia coli
mGDH
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
 Escherichia coli
pyrroloquinoline quinone coenzyme Escherichia coli

General Information

General Information Comment Organism
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