Literature summary 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.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.1.5.2	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

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

Synonyms

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

Cofactor

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

General Information

EC Number	General Information	Comment	Organism
1.1.5.2	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

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Release 2023.1 (January 2023)