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

BRENDA support

Literature summary for 1.1.5.2 extracted from

  • Mustafa, G.; Ishikawa, Y.; Kobayashi, K.; Migita, C.T.; Tagawa, S.; Yamada, M.
    Function of a bound ubiquinone in Escherichia coli quinoprotein glucose dehydrogenase (2008), Biofactors, 32, 23-29.
    View publication on PubMed
Search for more literature for 1.1.5.2

Protein Variants

Protein Variants Comment Organism
additional information studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function pulse radiolysis analysis reveal that the bound ubiquinone exists very close to pyrroloquinoline quinone at a distance of 11-13 A. Studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH Escherichia coli