Literature summary for 1.1.5.9 extracted from

Tsuruoka, N.; Sadakane, T.; Hayashi, R.; Tsujimura, S.
Bimolecular rate constants for FAD-dependent glucose dehydrogenase from Aspergillus terreus and organic electron Acceptors (2017), Int. J. Mol. Sci., 18, 604 .

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Organism

Organism	UniProt	Comment	Textmining
Aspergillus terreus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose + 1,2-naphthoquinone	an electrochemical method is applied to evaluate the bimolecular rate constants of selected electron acceptors. With regard to the formal potential, higher kcat/Km values are found for ortho-quinones (including 9,10-phenanthrenequinone and 1,2-naphthoquinone) than for para-quinones in the reaction with FAD-GDH. Thus, the mechanism for effective electron transfer can be explained by steric hindrance (the electron transfer distance between the FAD site and the redox site of the quinone molecules)	Aspergillus terreus	D-glucono-1,5-lactone + 1,2-naphthoquinol	-	?
D-glucose + 9,10-phenanthrenequinone	an electrochemical method is applied to evaluate the bimolecular rate constants of selected electron acceptors. With regard to the formal potential, higher kcat/Km values are found for ortho-quinones (including 9,10-phenanthrenequinone and 1,2-naphthoquinone) than for para-quinones in the reaction with FAD-GDH. Thus, the mechanism for effective electron transfer can be explained by steric hindrance (the electron transfer distance between the FAD site and the redox site of the quinone molecules)	Aspergillus terreus	D-glucono-1,5-lactone + 9,10-phenanthrenequinol	-	?

Synonyms

Synonyms	Comment	Organism
FAD-dependent glucose dehydrogenase	-	Aspergillus terreus
FAD-GDH	-	Aspergillus terreus
flavin adenine dinucleotide-dependent glucose dehydrogenase	-	Aspergillus terreus

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Release 2023.1 (January 2023)