Literature summary for 1.14.13.9 extracted from

Amaral, M.; Levy, C.; Heyes, D.J.; Lafite, P.; Outeiro, T.F.; Giorgini, F.; Leys, D.; Scrutton, N.S.
Structural basis of kynurenine 3-monooxygenase inhibition (2013), Nature, 496, 382-385.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in baculoviral system	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure, in the free form and in complex with the tight-binding inhibitor UPF 648. UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
UPF 648	UPF 648 binds close to the FAD cofactor and perturbs the local active site structure, preventing productive binding of the substrate kynurenine	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P38169	-	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Saccharomyces cerevisiae

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.000074	-	pH 8.0, 30°C	Saccharomyces cerevisiae	UPF 648

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Release 2023.1 (January 2023)