Literature summary for 1.6.3.1 extracted from

Hritz, J.; Zoldak, G.; Sedlak, E.
Cofactor assisted gating mechanism in the active site of NADH oxidase from Thermus thermophilus (2006), Proteins, 64, 465-476.

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Activating Compound

Activating Compound	Comment	Organism	Structure
Urea	increase of activity by 250% in presence of 1 M urea with no apparent perturbation in enzyme structure. Presence of urea prohibits the closing of the active site thus allowing the substrate to bind	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
NAD(P)H + H+ + O2 = NAD(P)+ + H2O2	in stable conformation, the active site adopts a closed conformation not allowing the substrate to bind. In presence of urea, an open conformation of the active site with 0.9 nm distance between the indole ring of W47 and the isoalloxazine ring of FMN412 is favored	Thermus thermophilus	a

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Release 2023.1 (January 2023)