Literature summary for 1.1.1.47 extracted from

Ulmer, W.; Froeschle, M.; Jany, K.D.
Evidence for an essential histidine residue in glucose dehydrogenase from Bacillus megaterium and sequence analysis of the peptides labeled with bromoacetyl pyridine (1983), Eur. J. Biochem., 136, 183-194.

Search for more literature for 1.1.1.47

Inhibitors

Inhibitors	Comment	Organism	Structure
3-(2-bromoacetyl)pyridine	active-site-directed irreverseible inhibitor, the cofactor NAD but not the substrate glucose protects the enzyme from the inactivation, in the presence of 0.1 M NAD and 1.37 mM 3-(2-bromoacetyl)pyridine, glucose dehydrogenase has still 85% of its original activity after incubation for 2 h	Priestia megaterium

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	P40288	-	-
Priestia megaterium IWG3	P40288	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose + NAD(P)+	-	Priestia megaterium	D-glucono-1,5-lactone + NAD(P)H	-	?
D-glucose + NAD(P)+	-	Priestia megaterium IWG3	D-glucono-1,5-lactone + NAD(P)H	-	?

Synonyms

Synonyms	Comment	Organism
glucose dehydrogenase	-	Priestia megaterium

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Priestia megaterium
NADP+	-	Priestia megaterium

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
7.7	-	3-(2-bromoacetyl)pyridine	-	Priestia megaterium

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)